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TBC1D14 regulates autophagy via the TRAPP complex and ATG9 traffic

https://doi.org/10.15252/embj.201592695

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/bies.201200130openalex-snapshot

Endocytosis and autophagy: Shared machinery for degradation

inferredcites →https://doi.org/10.1002/prot.21885openalex-snapshot

First crystallographic models of human TBC domains in the context of a family‐wide structural analysis

inferredcites →https://doi.org/10.1016/0092-8674(92)90643-qopenalex-snapshot

Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases

inferredcites →https://doi.org/10.1016/0092-8674(94)90570-3openalex-snapshot

RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs

inferredcites →https://doi.org/10.1016/j.cell.2005.06.043openalex-snapshot

Rab Conversion as a Mechanism of Progression from Early to Late Endosomes

inferredcites →https://doi.org/10.1016/j.cell.2011.06.023openalex-snapshot

Autophagosome Precursor Maturation Requires Homotypic Fusion

inferredcites →https://doi.org/10.1016/j.cell.2012.11.001openalex-snapshot

The Hairpin-type Tail-Anchored SNARE Syntaxin 17 Targets to Autophagosomes for Fusion with Endosomes/Lysosomes

inferredcites →https://doi.org/10.1016/j.cell.2013.01.030openalex-snapshot

A Systematic Mammalian Genetic Interaction Map Reveals Pathways Underlying Ricin Susceptibility

inferredcites →https://doi.org/10.1016/j.cell.2013.08.044openalex-snapshot

Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes

inferredcites →https://doi.org/10.1016/j.febslet.2010.01.020openalex-snapshot

New insights into the function of Atg9

inferredcites →https://doi.org/10.1016/j.molcel.2013.12.011openalex-snapshot

Early Steps in Autophagy Depend on Direct Phosphorylation of Atg9 by the Atg1 Kinase

inferredcites →https://doi.org/10.1016/j.molcel.2014.05.021openalex-snapshot

WIPI2 Links LC3 Conjugation with PI3P, Autophagosome Formation, and Pathogen Clearance by Recruiting Atg12–5-16L1

inferredcites →https://doi.org/10.1021/jm101144fopenalex-snapshot

Discovery of 1-(4-(4-Propionylpiperazin-1-yl)-3-(trifluoromethyl)phenyl)-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one as a Highly Potent, Selective Mammalian Target of Rapamycin (mTOR) Inhibitor for the Treatment of Cancer

inferredcites →https://doi.org/10.1034/j.1600-0854.2003.00103.xopenalex-snapshot

Golgin‐84 is a rab1 Binding Partner Involved in Golgi Structure

inferredcites →https://doi.org/10.1038/nature06639openalex-snapshot

Autophagy fights disease through cellular self-digestion

inferredcites →https://doi.org/10.1038/nature09204openalex-snapshot

Network organization of the human autophagy system

inferredcites →https://doi.org/10.1038/nature10098openalex-snapshot

Global quantification of mammalian gene expression control

inferredcites →https://doi.org/10.1038/nature11910openalex-snapshot

Autophagosomes form at ER–mitochondria contact sites

inferredcites →https://doi.org/10.1038/ncb1740openalex-snapshot

Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking

inferredcites →https://doi.org/10.1038/ncb1991openalex-snapshot

A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation

inferredcites →https://doi.org/10.1038/ncb2078openalex-snapshot

Plasma membrane contributes to the formation of pre-autophagosomal structures

inferredcites →https://doi.org/10.1038/ncomms5998openalex-snapshot

PICALM modulates autophagy activity and tau accumulation

inferredcites →https://doi.org/10.1038/nrm2999openalex-snapshot

TRAPP complexes in membrane traffic: convergence through a common Rab

inferredcites →https://doi.org/10.1038/nrm3267openalex-snapshot

Illuminating the functional and structural repertoire of human TBC/RABGAPs

inferredcites →https://doi.org/10.1038/nrm3364openalex-snapshot

Illuminating the functional and structural repertoire of human TBC/RABGAPs

inferredcites →https://doi.org/10.1038/nrm3696openalex-snapshot

The autophagosome: origins unknown, biogenesis complex

inferredcites →https://doi.org/10.1073/pnas.1000063107openalex-snapshot

Trs85 directs a Ypt1 GEF, TRAPPIII, to the phagophore to promote autophagy

inferredcites →https://doi.org/10.1073/pnas.1121299109openalex-snapshot

Regulation of selective autophagy onset by a Ypt/Rab GTPase module

inferredcites →https://doi.org/10.1073/pnas.1302337110openalex-snapshot

Ypt1 recruits the Atg1 kinase to the preautophagosomal structure

inferredcites →https://doi.org/10.1073/pnas.1316356110openalex-snapshot

The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway

inferredcites →https://doi.org/10.1074/jbc.273.51.33889openalex-snapshot

A New Protein Conjugation System in Human

inferredcites →https://doi.org/10.1074/jbc.m112.395087openalex-snapshot

Phosphatidylinositol 3-Phosphatase Myotubularin-related Protein 6 (MTMR6) Is Regulated by Small GTPase Rab1B in the Early Secretory and Autophagic Pathways

inferredcites →https://doi.org/10.1074/jbc.m112.411454openalex-snapshot

Atg9 Vesicles Recruit Vesicle-tethering Proteins Trs85 and Ypt1 to the Autophagosome Formation Site

inferredcites →https://doi.org/10.1074/jbc.m703663200openalex-snapshot

siRNA Screening of the Kinome Identifies ULK1 as a Multidomain Modulator of Autophagy

inferredcites →https://doi.org/10.1080/15548627.2015.1017178openalex-snapshot

Ultrastructural relationship of the phagophore with surrounding organelles

inferredcites →https://doi.org/10.1083/jcb.200207045openalex-snapshot

The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation

inferredcites →https://doi.org/10.1083/jcb.200712064openalex-snapshot

FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells

inferredcites →https://doi.org/10.1083/jcb.200803137openalex-snapshot

Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum

inferredcites →https://doi.org/10.1083/jcb.201003122openalex-snapshot

α-Synuclein impairs macroautophagy: implications for Parkinson’s disease

inferredcites →https://doi.org/10.1083/jcb.201008107openalex-snapshot

OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation

inferredcites →https://doi.org/10.1083/jcb.201110114openalex-snapshot

Arf6 promotes autophagosome formation via effects on phosphatidylinositol 4,5-bisphosphate and phospholipase D

inferredcites →https://doi.org/10.1083/jcb.201111079openalex-snapshot

TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes

inferredcites →https://doi.org/10.1083/jcb.201112098openalex-snapshot

A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells

inferredcites →https://doi.org/10.1083/jcb.201202061openalex-snapshot

Atg9 vesicles are an important membrane source during early steps of autophagosome formation

inferredcites →https://doi.org/10.1083/jcb.201205129openalex-snapshot

Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation

inferredcites →https://doi.org/10.1091/mbc.e02-09-0625openalex-snapshot

COPI Recruitment Is Modulated by a Rab1b-dependent Mechanism

inferredcites →https://doi.org/10.1091/mbc.e05-05-0447openalex-snapshot

Cis-Golgi Matrix Proteins Move Directly to Endoplasmic Reticulum Exit Sites by Association with Tubules

inferredcites →https://doi.org/10.1091/mbc.e07-12-1231openalex-snapshot

Golgi-resident Small GTPase Rab33B Interacts with Atg16L and Modulates Autophagosome Formation

inferredcites →https://doi.org/10.1091/mbc.e08-12-1229openalex-snapshot

The Function of the Intermediate Compartment in Pre-Golgi Trafficking Involves its Stable Connection with the Centrosome

inferredcites →https://doi.org/10.1091/mbc.e09-05-0387openalex-snapshot

mTrs130 Is a Component of a Mammalian TRAPPII Complex, a Rab1 GEF That Binds to COPI-coated Vesicles

inferredcites →https://doi.org/10.1091/mbc.e10-05-0392openalex-snapshot

Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex

inferredcites →https://doi.org/10.1091/mbc.e10-11-0873openalex-snapshot

C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking

inferredcites →https://doi.org/10.1091/mbc.e11-09-0746openalex-snapshot

Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy

inferredcites →https://doi.org/10.1091/mbc.e13-07-0381openalex-snapshot

ER exit sites are physical and functional core autophagosome biogenesis components

inferredcites →https://doi.org/10.1093/emboj/17.9.2494openalex-snapshot

TRAPP, a highly conserved novel complex on the cis‐Golgi that mediates vesicle docking and fusion

inferredcites →https://doi.org/10.1093/emboj/19.21.5720openalex-snapshot

LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing

inferredcites →https://doi.org/10.1111/j.1600-0854.2010.01086.xopenalex-snapshot

Autophagosome Formation Depends on the Small GTPase Rab1 and Functional ER Exit Sites

inferredcites →https://doi.org/10.1111/j.1600-0854.2010.01087.xopenalex-snapshot

A Targeted siRNA Screen to Identify SNAREs Required for Constitutive Secretion in Mammalian Cells

inferredcites →https://doi.org/10.1111/tra.12024openalex-snapshot

Trs130 Participates in Autophagy Through GTPases Ypt31/32 in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1128/mcb.01082-08openalex-snapshot

Kinase-Inactivated ULK Proteins Inhibit Autophagy via Their Conserved C-Terminal Domains Using an Atg13-Independent Mechanism

inferredcites →https://doi.org/10.1128/mcb.06717-11openalex-snapshot

Rab GTPase-Activating Proteins in Autophagy: Regulation of Endocytic and Autophagy Pathways by Direct Binding to Human ATG8 Modifiers

inferredcites →https://doi.org/10.1159/000350326openalex-snapshot

Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila

inferredcites →https://doi.org/10.1159/000373980openalex-snapshot

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

inferredcites →https://doi.org/10.1159/000479571openalex-snapshot

Induction of the Vitamin D Receptor Attenuates Autophagy Dysfunction-Mediated Cell Death Following Traumatic Brain Injury

inferredcites →https://doi.org/10.1186/1471-2156-11-106openalex-snapshot

High resolution mapping and positional cloning of ENU-induced mutations in the Rw region of mouse chromosome 5

inferredcites →https://doi.org/10.1242/jcs.00381openalex-snapshot

Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate

inferredcites →https://doi.org/10.1242/jcs.01131openalex-snapshot

LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation

inferredcites →https://doi.org/10.1242/jcs.014225openalex-snapshot

Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells

inferredcites →https://doi.org/10.1242/jcs.03172openalex-snapshot

Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes

inferredcites →https://doi.org/10.1242/jcs.126128openalex-snapshot

The LIR motif – crucial for selective autophagy

inferredcites →https://doi.org/10.1242/jcs.131318openalex-snapshot

TRAPPIII is responsible for the vesicular transport from early endosomes to the Golgi apparatus that facilitates Atg9 cycling in autophagy

inferredcites →https://doi.org/10.1242/jcs.132415openalex-snapshot

Dynamic association of the ULK1 complex with omegasomes during autophagy induction

inferredcites →https://doi.org/10.1371/journal.pone.0080297openalex-snapshot

Identification of TRAPPC8 as a Host Factor Required for Human Papillomavirus Cell Entry

inferredcites →https://doi.org/10.15252/embj.201592695openalex-snapshot

TBC1D14 regulates autophagy via the TRAPP complex and ATG9 traffic

inferredcites →https://doi.org/10.4161/auto.1.1.1512openalex-snapshot

Early Secretory Pathway GeneTRS85is Required for Selective Macroautophagy of Peroxisomes inYarrowia lipolytica

inferredcites →https://doi.org/10.4161/auto.19496openalex-snapshot

Guidelines for the use and interpretation of assays for monitoring autophagy

inferredcites →https://doi.org/10.4161/auto.25529openalex-snapshot

Temporal analysis of recruitment of mammalian ATG proteins to the autophagosome formation site

inferredcites →https://doi.org/10.4161/auto.5.5.8249openalex-snapshot

A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy

inferredcites →https://doi.org/10.4161/auto.5.7.9296openalex-snapshot

Atg101, a novel mammalian autophagy protein interacting with Atg13

inferredcites →https://doi.org/10.4161/auto.5.8.10274openalex-snapshot

3D tomography reveals connections between the phagophore and endoplasmic reticulum

inferredcites →https://doi.org/10.4161/auto.6.4.11863openalex-snapshot

Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation

inferredcites →https://doi.org/10.4161/auto.7.1.13840openalex-snapshot

Antibacterial autophagy occurs at PI(3)P-enriched domains of the endoplasmic reticulum and requires Rab1 GTPase

inferredcites →https://doi.org/10.7554/elife.00947openalex-snapshot

The ER–Golgi intermediate compartment is a key membrane source for the LC3 lipidation step of autophagosome biogenesis

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Nondegradable Ubiquitinated ATG9A Organizes Golgi Integrity and Dynamics Upon Stresses

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Mammalian Atg9 contributes to the post‐Golgi transport of lysosomal hydrolases by interacting with adaptor protein‐1

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Hijacking intracellular membranes to feed autophagosomal growth

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The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11

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The TRAPP complexes: discriminating GTPases in context

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A conserved glycine residue in the C-terminal region of human ATG9A is required for its transport from the endoplasmic reticulum to the Golgi apparatus

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Establishment of the phagophore–ERES membrane contact site initiates phagophore elongation

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Interaction of TBC1D9B with Mammalian ATG8 Homologues Regulates Autophagic Flux

inferred← citeshttps://doi.org/10.1038/s41598-019-50415-6openalex-snapshot

Characterization of three TRAPPC11 variants suggests a critical role for the extreme carboxy terminus of the protein

inferred← citeshttps://doi.org/10.1038/s44319-026-00908-zopenalex-snapshot

The ER–Golgi intermediate compartment: a central hub integrating membrane trafficking and stress responses

inferred← citeshttps://doi.org/10.1042/bst20170128openalex-snapshot

Autophagy in the context of the cellular membrane-trafficking system: the enigma of Atg9 vesicles

inferred← citeshttps://doi.org/10.1073/pnas.1705572114openalex-snapshot

SNARE priming is essential for maturation of autophagosomes but not for their formation

inferred← citeshttps://doi.org/10.1073/pnas.1814552115openalex-snapshot

Noncanonical autophagy at ER exit sites regulates procollagen turnover

inferred← citeshttps://doi.org/10.1080/14789450.2017.1365603openalex-snapshot

Insights from protein-protein interaction studies on bacterial pathogenesis

inferred← citeshttps://doi.org/10.1080/15384101.2016.1176400openalex-snapshot

TBC1D14 and TRAPP – Regulating autophagy through ATG9

inferred← citeshttps://doi.org/10.1080/15548627.2017.1359381openalex-snapshot

Architecture of the ATG2B-WDR45 complex and an aromatic Y/HF motif crucial for complex formation

inferred← citeshttps://doi.org/10.1080/15548627.2017.1378838openalex-snapshot

Autophagy pathway: Cellular and molecular mechanisms

inferred← citeshttps://doi.org/10.1080/15548627.2018.1477382openalex-snapshot

Atg9 proteins, not so different after all

inferred← citeshttps://doi.org/10.1080/15548627.2019.1569929openalex-snapshot

Gyp1 has a dual function as Ypt1 GAP and interaction partner of Atg8 in selective autophagy

inferred← citeshttps://doi.org/10.1080/15548627.2019.1596478openalex-snapshot

RAB2 regulates the formation of autophagosome and autolysosome in mammalian cells

inferred← citeshttps://doi.org/10.1080/15548627.2020.1847461openalex-snapshot

Protein complexes and neighborhoods driving autophagy

inferred← citeshttps://doi.org/10.1080/15548627.2024.2367907openalex-snapshot

TBC1D4 antagonizes RAB2A-mediated autophagic and endocytic pathways

inferred← citeshttps://doi.org/10.1080/15592294.2023.2257538openalex-snapshot

ATG9A modulated by miR-195-5p can boost the malignant progression of cervical cancer cells

inferred← citeshttps://doi.org/10.1080/21541248.2016.1220779openalex-snapshot

Rabs and GAPs in starvation-induced autophagy

inferred← citeshttps://doi.org/10.1080/21541248.2016.1246280openalex-snapshot

Small GTPase proteins in macroautophagy

inferred← citeshttps://doi.org/10.1080/21541248.2016.1258444openalex-snapshot

Small GTPases controlling autophagy-related membrane traffic in yeast and metazoans

inferred← citeshttps://doi.org/10.1080/21541248.2017.1346553openalex-snapshot

Multifaceted role of SMCR8 as autophagy regulator

inferred← citeshttps://doi.org/10.1080/27694127.2022.2042054openalex-snapshot

The ATG5 interactome links clathrin-mediated vesicular trafficking with the autophagosome assembly machinery

inferred← citeshttps://doi.org/10.1083/jcb.201705214openalex-snapshot

The TRAPPIII complex activates the GTPase Ypt1 (Rab1) in the secretory pathway

inferred← citeshttps://doi.org/10.1083/jcb.201901115openalex-snapshot

ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIIβ

inferred← citeshttps://doi.org/10.1083/jcb.202601107openalex-snapshot

The Rab GEF VINE couples phosphatase recruitment to GAP-mediated Rab5 inactivation

inferred← citeshttps://doi.org/10.1091/mbc.e24-12-0535openalex-snapshot

Trafficking of K63-polyubiquitin–modified membrane proteins in a macroautophagy-independent pathway is linked to ATG9A

inferred← citeshttps://doi.org/10.1093/brain/awaa046openalex-snapshot

Recurrent bi-allelic splicing variant c.454+3A>G in TRAPPC4 is associated with progressive encephalopathy and muscle involvement

inferred← citeshttps://doi.org/10.1093/brain/awz374openalex-snapshot

Deficiencies in vesicular transport mediated by TRAPPC4 are associated with severe syndromic intellectual disability

inferred← citeshttps://doi.org/10.1093/plphys/kiae426openalex-snapshot

How coat proteins shape autophagy in plant cells

inferred← citeshttps://doi.org/10.1093/plphys/kiaf042openalex-snapshot

The TRAPPC8/TRS85 subunit of the Arabidopsis TRAPPIII tethering complex regulates endoplasmic reticulum function and autophagy

inferred← citeshttps://doi.org/10.1097/cm9.0000000000001797openalex-snapshot

Selective elimination of host cells harboring replication-competent human immunodeficiency virus reservoirs: a promising therapeutic strategy for HIV cure

inferred← citeshttps://doi.org/10.1101/2020.05.05.079970openalex-snapshot

Splicing variation of BMP2K balances endocytosis, COPII trafficking and autophagy in erythroid cells

inferred← citeshttps://doi.org/10.1101/2020.10.08.332312openalex-snapshot

Structure and mechanism of TRAPPIII-mediated Rab1 activation

inferred← citeshttps://doi.org/10.1101/2024.01.11.575191openalex-snapshot

The Arabidopsis thaliana TRAPPIII subunit AtTRAPPC8/AtTRS85 is involved in ER functioning and autophagy

inferred← citeshttps://doi.org/10.1101/769059openalex-snapshot

The ATG5 Interactome Links Clathrin Vesicular Trafficking With The ATG8 Lipidation Machinery For Autophagosome Assembly

inferred← citeshttps://doi.org/10.1105/tpc.20.00044openalex-snapshot

TRIPP Is a Plant-Specific Component of the Arabidopsis TRAPPII Membrane Trafficking Complex with Important Roles in Plant Development

inferred← citeshttps://doi.org/10.1111/febs.13931openalex-snapshot

Mammalian autophagy and the plasma membrane

inferred← citeshttps://doi.org/10.1111/jnc.15194openalex-snapshot

Mechanisms of neuronal survival safeguarded by endocytosis and autophagy

inferred← citeshttps://doi.org/10.1111/joim.12596openalex-snapshot

Role of autophagy in HIV infection and pathogenesis

inferred← citeshttps://doi.org/10.1111/nan.12690openalex-snapshot

Novel autophagic vacuolar myopathies: Phenotype and genotype features

inferred← citeshttps://doi.org/10.1111/tpj.14442openalex-snapshot

Interactions between Transport Protein Particle (TRAPP) complexes and Rab GTP ases in Arabidopsis

inferred← citeshttps://doi.org/10.1111/tra.12615openalex-snapshot

TRAPPopathies: An emerging set of disorders linked to variations in the genes encoding transport protein particle (TRAPP)‐associated proteins

inferred← citeshttps://doi.org/10.1111/tra.12640openalex-snapshot

TRAPPC11 functions in autophagy by recruiting ATG2B‐WIPI4/WDR45 to preautophagosomal membranes

inferred← citeshttps://doi.org/10.1111/tra.70001openalex-snapshot

Disease‐Associated Factors at the Endoplasmic Reticulum–Golgi Interface

inferred← citeshttps://doi.org/10.1126/sciadv.aay4624openalex-snapshot

Integrated proteogenetic analysis reveals the landscape of a mitochondrial-autophagosome synapse during PARK2-dependent mitophagy

inferred← citeshttps://doi.org/10.1126/sciadv.adg2997openalex-snapshot

Structural basis for ATG9A recruitment to the ULK1 complex in mitophagy initiation

inferred← citeshttps://doi.org/10.1136/jmedgenet-2018-105441openalex-snapshot

Bi-allelic mutations in TRAPPC2L result in a neurodevelopmental disorder and have an impact on RAB11 in fibroblasts

inferred← citeshttps://doi.org/10.1146/annurev-biochem-061516-044820openalex-snapshot

Mechanisms of Autophagy Initiation

inferred← citeshttps://doi.org/10.1146/annurev-genet-030620-102906openalex-snapshot

Moonlighting Proteins

inferred← citeshttps://doi.org/10.1155/2018/4541538openalex-snapshot

Rab GTPases in Osteoclastic Endomembrane Systems

inferred← citeshttps://doi.org/10.1155/2020/1953242openalex-snapshot

miR‐146b‐5p Plays a Critical Role in the Regulation of Autophagy in ∆per Brucella melitensis‐Infected RAW264.7 Cells

inferred← citeshttps://doi.org/10.1177/17590914221142360openalex-snapshot

Rab11 and Its Role in Neurodegenerative Diseases

inferred← citeshttps://doi.org/10.1186/s12964-025-02317-6openalex-snapshot

Progress on multifunctional transmembrane protein ATG9A

inferred← citeshttps://doi.org/10.1186/s13578-020-00467-3openalex-snapshot

Autophagy and its role in regeneration and remodeling within invertebrate

inferred← citeshttps://doi.org/10.1189/jlb.4mr0216-079ropenalex-snapshot

Autophagy in leukocytes and other cells: mechanisms, subsystem organization, selectivity, and links to innate immunity

inferred← citeshttps://doi.org/10.1242/jcs.196196openalex-snapshot

Atg9A trafficking through the recycling endosomes is required for autophagosome formation

inferred← citeshttps://doi.org/10.1242/jcs.199521openalex-snapshot

TRAPPC13 modulates autophagy and the response to Golgi stress

inferred← citeshttps://doi.org/10.1242/jcs.216630openalex-snapshot

TBC1D5 controls the GTPase cycle of Rab7b

inferred← citeshttps://doi.org/10.1242/jcs.250670openalex-snapshot

The phosphatidylinositol 3-phosphate-binding protein SNX4 controls ATG9A recycling and autophagy

inferred← citeshttps://doi.org/10.1247/csf.16008openalex-snapshot

Multiple Types of Guanine Nucleotide Exchange Factors (GEFs) for Rab Small GTPases

inferred← citeshttps://doi.org/10.1371/journal.pone.0174883openalex-snapshot

TBC1D12 is a novel Rab11-binding protein that modulates neurite outgrowth of PC12 cells

inferred← citeshttps://doi.org/10.1371/journal.ppat.1008220openalex-snapshot

A trafficome-wide RNAi screen reveals deployment of early and late secretory host proteins and the entire late endo-/lysosomal vesicle fusion machinery by intracellular Salmonella

inferred← citeshttps://doi.org/10.15252/embj.201694866openalex-snapshot

COPI–TRAPPII activates Rab18 and regulates its lipid droplet association

inferred← citeshttps://doi.org/10.15252/embj.201695081openalex-snapshot

Dedicated SNAREs and specialized TRIM cargo receptors mediate secretory autophagy

inferred← citeshttps://doi.org/10.15252/embj.201695189openalex-snapshot

Autophagosome formation is initiated at phosphatidylinositol synthase‐enriched ER subdomains

inferred← citeshttps://doi.org/10.15252/embj.201696287openalex-snapshot

TRAPPing Rab18 in lipid droplets

inferred← citeshttps://doi.org/10.15252/embj.201796463openalex-snapshot

Rab35 GTPase recruits NDP52 to autophagy targets

inferred← citeshttps://doi.org/10.15252/embj.2019101704openalex-snapshot

The TRAPP complex mediates secretion arrest induced by stress granule assembly

inferred← citeshttps://doi.org/10.15252/embj.2020107607openalex-snapshot

Structural basis of TRAPPIII‐mediated Rab1 activation

inferred← citeshttps://doi.org/10.15252/embj.2020107608openalex-snapshot

Cryo‐EM structure of metazoan TRAPPIII, the multi‐subunit complex that activates the GTPase Rab1

inferred← citeshttps://doi.org/10.15252/embr.201744559openalex-snapshot

Remodeling of ER‐exit sites initiates a membrane supply pathway for autophagosome biogenesis

inferred← citeshttps://doi.org/10.15252/embr.201744837openalex-snapshot

SNX18 regulates ATG9A trafficking from recycling endosomes by recruiting Dynamin‐2

inferred← citeshttps://doi.org/10.15252/embr.202051136openalex-snapshot

BioID reveals an ATG9A interaction with ATG13-ATG101 in the degradation of p62/SQSTM1-ubiquitin clusters

inferred← citeshttps://doi.org/10.20517/evcna.2025.21openalex-snapshot

Extracellular vesicles: cargo loading, degradation and secretory pathways, and their intersection with autophagy

inferred← citeshttps://doi.org/10.24998/maeusabed.355164openalex-snapshot

Memeli hücrelerinde otofajinin moleküler mekanizması

inferred← citeshttps://doi.org/10.3389/fcell.2016.00028openalex-snapshot

Spatial and Functional Aspects of ER-Golgi Rabs and Tethers

inferred← citeshttps://doi.org/10.3389/fcell.2019.00171openalex-snapshot

A New Look at the Functional Organization of the Golgi Ribbon

inferred← citeshttps://doi.org/10.3389/fcell.2020.00148openalex-snapshot

Distinct Roles of TRAPPC8 and TRAPPC12 in Ciliogenesis via Their Interactions With OFD1

inferred← citeshttps://doi.org/10.3389/fcell.2020.564975openalex-snapshot

Golgi Apparatus: A Potential Therapeutic Target for Autophagy-Associated Neurological Diseases

inferred← citeshttps://doi.org/10.3389/fcell.2023.1069256openalex-snapshot

Impact of interorganelle coordination between the conventional early secretory pathway and autophagy in cellular homeostasis and stress response

inferred← citeshttps://doi.org/10.3389/fnmol.2017.00143openalex-snapshot

Autophagy as an Emerging Common Pathomechanism in Inherited Peripheral Neuropathies

inferred← citeshttps://doi.org/10.3389/fnsyn.2022.829354openalex-snapshot

Organization of Presynaptic Autophagy-Related Processes

inferred← citeshttps://doi.org/10.3389/fpls.2020.00565openalex-snapshot

Recent Advances in Membrane Shaping for Plant Autophagosome Biogenesis

inferred← citeshttps://doi.org/10.3389/fpsyt.2023.1065417openalex-snapshot

Co-expression network of mRNA and DNA methylation in first-episode and drug-naive adolescents with major depressive disorder

inferred← citeshttps://doi.org/10.3389/fvets.2022.909039openalex-snapshot

Genome-Wide Detection of Copy Number Variations and Evaluation of Candidate Copy Number Polymorphism Genes Associated With Complex Traits of Pigs

inferred← citeshttps://doi.org/10.3389/fvets.2022.983562openalex-snapshot

Non-coding transcriptomic profiles in the sheep mammary gland during different lactation periods

inferred← citeshttps://doi.org/10.3390/cells10112814openalex-snapshot

Key Regulators of Autophagosome Closure

inferred← citeshttps://doi.org/10.3390/cells11050780openalex-snapshot

Maintaining Golgi Homeostasis: A Balancing Act of Two Proteolytic Pathways

inferred← citeshttps://doi.org/10.3390/cells5020024openalex-snapshot

Advances in Autophagy Regulatory Mechanisms

inferred← citeshttps://doi.org/10.3390/cells8030224openalex-snapshot

Rab7a and Mitophagosome Formation

inferred← citeshttps://doi.org/10.3390/ijms222112087openalex-snapshot

Focus on the Small GTPase Rab1: A Key Player in the Pathogenesis of Parkinson’s Disease

inferred← citeshttps://doi.org/10.3410/f.728773296.793572492openalex-snapshot

Faculty Opinions recommendation of Architecture of the ATG2B-WDR45 complex and an aromatic Y/HF motif crucial for complex formation.

inferred← citeshttps://doi.org/10.3410/f.735412929.793562076openalex-snapshot

Faculty Opinions recommendation of ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIIβ.

inferred← citeshttps://doi.org/10.70675/b16b80e6z881ez455cz9249z74e6c1530a78openalex-snapshot

Contrôle du développement et de la progression du carcinome hépatocellulaire par l’autophagie des macrophages : rôle du micro-environnement immunitaire

inferred← citeshttps://doi.org/10.7150/ijbs.68992openalex-snapshot

TBC1D14 inhibits autophagy to suppress lymph node metastasis in head and neck squamous cell carcinoma by downregulating macrophage erythroblast attacher

inferred← citeshttps://doi.org/10.7150/thno.30224openalex-snapshot

TBC1D8 Amplification Drives Tumorigenesis through Metabolism Reprogramming in Ovarian Cancer

inferred← citeshttps://doi.org/10.7554/elife.107316.2openalex-snapshot

ATG2A engages RAB1A and ARFGAP1 positive membranes during autophagosome biogenesis

inferred← citeshttps://doi.org/10.7554/elife.23063openalex-snapshot

Multiplex image-based autophagy RNAi screening identifies SMCR8 as ULK1 kinase activity and gene expression regulator

inferred← citeshttps://doi.org/10.7554/elife.29338openalex-snapshot

Atg9 antagonizes TOR signaling to regulate intestinal cell growth and epithelial homeostasis in Drosophila

inferred← citeshttps://doi.org/10.7554/elife.31326openalex-snapshot

Endosomal Rab cycles regulate Parkin-mediated mitophagy

inferred← citeshttps://doi.org/10.7554/elife.58504openalex-snapshot

Splicing variation of BMP2K balances abundance of COPII assemblies and autophagic degradation in erythroid cells

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