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FIP200 organizes the autophagy machinery at p62-ubiquitin condensates beyond activation of the ULK1 kinase

https://doi.org/10.1101/2020.07.07.191189

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What this work says

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

inferredcites →https://doi.org/10.1006/bbrc.1998.8546openalex-snapshot

Identification of Mouse ULK1, a Novel Protein Kinase Structurally Related toC. elegansUNC-51

inferredcites →https://doi.org/10.1016/j.cell.2018.09.048openalex-snapshot

Biological Functions of Autophagy Genes: A Disease Perspective

inferredcites →https://doi.org/10.1016/j.devcel.2017.11.024openalex-snapshot

CCPG1 Is a Non-canonical Autophagy Cargo Receptor Essential for ER-Phagy and Pancreatic ER Proteostasis

inferredcites →https://doi.org/10.1016/j.devcel.2019.06.016openalex-snapshot

Selective Autophagy of Mitochondria on a Ubiquitin-Endoplasmic-Reticulum Platform

inferredcites →https://doi.org/10.1016/j.jmb.2016.02.004openalex-snapshot

Mechanisms of Selective Autophagy

inferredcites →https://doi.org/10.1016/j.jmb.2019.07.027openalex-snapshot

Recruitment and Activation of the ULK1/Atg1 Kinase Complex in Selective Autophagy

inferredcites →https://doi.org/10.1016/j.molcel.2011.07.039openalex-snapshot

Serine 403 Phosphorylation of p62/SQSTM1 Regulates Selective Autophagic Clearance of Ubiquitinated Proteins

inferredcites →https://doi.org/10.1016/j.molcel.2013.08.003openalex-snapshot

Phosphorylation of p62 Activates the Keap1-Nrf2 Pathway during Selective Autophagy

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/10.1016/j.molcel.2015.05.031openalex-snapshot

Small Molecule Inhibition of the Autophagy Kinase ULK1 and Identification of ULK1 Substrates

inferredcites →https://doi.org/10.1016/j.molcel.2019.01.035openalex-snapshot

FIP200 Claw Domain Binding to p62 Promotes Autophagosome Formation at Ubiquitin Condensates

inferredcites →https://doi.org/10.1016/j.molcel.2019.01.041openalex-snapshot

The Cargo Receptor NDP52 Initiates Selective Autophagy by Recruiting the ULK Complex to Cytosol-Invading Bacteria

inferredcites →https://doi.org/10.1016/j.molcel.2019.02.010openalex-snapshot

Spatiotemporal Control of ULK1 Activation by NDP52 and TBK1 during Selective Autophagy

inferredcites →https://doi.org/10.1038/26506openalex-snapshot

A protein conjugation system essential for autophagy

inferredcites →https://doi.org/10.1038/35044114openalex-snapshot

A ubiquitin-like system mediates protein lipidation

inferredcites →https://doi.org/10.1038/nbt.2647openalex-snapshot

DNA targeting specificity of RNA-guided Cas9 nucleases

inferredcites →https://doi.org/10.1038/ncb1007-1102openalex-snapshot

Autophagosome formation: core machinery and adaptations

inferredcites →https://doi.org/10.1038/ncb1846openalex-snapshot

Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages

inferredcites →https://doi.org/10.1038/ncb2757openalex-snapshot

ULK1 induces autophagy by phosphorylating Beclin-1 and activating VPS34 lipid kinase

inferredcites →https://doi.org/10.1038/ncomms12420openalex-snapshot

Autophagy initiation by ULK complex assembly on ER tubulovesicular regions marked by ATG9 vesicles

inferredcites →https://doi.org/10.1038/s41421-020-0155-1openalex-snapshot

Activation and targeting of ATG8 protein lipidation

inferredcites →https://doi.org/10.1038/s41422-018-0017-7openalex-snapshot

Polyubiquitin chain-induced p62 phase separation drives autophagic cargo segregation

inferredcites →https://doi.org/10.1042/bj20101894openalex-snapshot

The serine/threonine kinase ULK1 is a target of multiple phosphorylation events

inferredcites →https://doi.org/10.1074/jbc.273.7.3963openalex-snapshot

Tor, a Phosphatidylinositol Kinase Homologue, Controls Autophagy in Yeast

inferredcites →https://doi.org/10.1074/jbc.c114.627778openalex-snapshot

Pharmacological Inhibition of ULK1 Kinase Blocks Mammalian Target of Rapamycin (mTOR)-dependent Autophagy

inferredcites →https://doi.org/10.1074/jbc.m900573200openalex-snapshot

ULK1·ATG13·FIP200 Complex Mediates mTOR Signaling and Is Essential for Autophagy

inferredcites →https://doi.org/10.1080/15548627.2016.1140293openalex-snapshot

The ULK1 complex mediates MTORC1 signaling to the autophagy initiation machinery via binding and phosphorylating ATG14

inferredcites →https://doi.org/10.1083/jcb.200507002openalex-snapshot

p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death

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.201811139openalex-snapshot

ATG2 transports lipids to promote autophagosome biogenesis

inferredcites →https://doi.org/10.1083/jcb.201911047openalex-snapshot

ULK complex organization in autophagy by a C-shaped FIP200 N-terminal domain dimer

inferredcites →https://doi.org/10.1083/jcb.202002085openalex-snapshot

Autophagosome biogenesis: From membrane growth to closure

inferredcites →https://doi.org/10.1091/mbc.e05-09-0841openalex-snapshot

Assortment of Phosphatidylinositol 3-Kinase Complexes—Atg14p Directs Association of Complex I to the Pre-autophagosomal Structure inSaccharomyces cerevisiae

inferredcites →https://doi.org/10.1091/mbc.e08-12-1248openalex-snapshot

Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy

inferredcites →https://doi.org/10.1091/mbc.e08-12-1249openalex-snapshot

ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery

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/10.1101/558767openalex-snapshot

Selective autophagic clearance of protein aggregates is mediated by the autophagy receptor, TAX1BP1

inferredcites →https://doi.org/10.1101/712828openalex-snapshot

Super-resolution microscopy unveils FIP200-scaffolded, cup-shaped organization of mammalian autophagic initiation machinery

inferredcites →https://doi.org/10.1128/mcb.06159-11openalex-snapshot

Role of AMPK-mTOR-Ulk1/2 in the Regulation of Autophagy: Cross Talk, Shortcuts, and Feedbacks

inferredcites →https://doi.org/10.1146/annurev-biochem-061516-044820openalex-snapshot

Mechanisms of Autophagy Initiation

inferredcites →https://doi.org/10.1146/annurev-cellbio-100818-125300openalex-snapshot

Diverse Cellular Roles of Autophagy

inferredcites →https://doi.org/10.1186/s13024-016-0141-0openalex-snapshot

ULK1-mediated phosphorylation of ATG14 promotes autophagy and is impaired in Huntington’s disease models

inferredcites →https://doi.org/10.1242/jcs.146258openalex-snapshot

WIPI proteins: essential PtdIns3 P effectors at the nascent autophagosome

inferredcites →https://doi.org/10.1242/jcs.156034openalex-snapshot

Ultrastructural analysis of autophagosome organization using mammalian autophagy-deficient cells

inferredcites →https://doi.org/10.1242/jcs.214304openalex-snapshot

p62-mediated phase separation at the intersection of the ubiquitin-proteasome system and autophagy

inferredcites →https://doi.org/10.15252/embj.201798308openalex-snapshot

p62 filaments capture and present ubiquitinated cargos for autophagy

inferredcites →https://doi.org/10.18632/oncotarget.26295openalex-snapshot

Serum starvation raises turnover of phosphorylated p62/SQSTM1 (Serine 349), reveals expression of proteasome and N-glycanase1 interactive protein RAD23B and sensitizes human synovial fibroblasts to BAY 11-7085-induced cell death

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.5.4.8062openalex-snapshot

Atg14 and UVRAG: Mutually exclusive subunits of mammalian Beclin 1-PI3K complexes

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.6.6.12709openalex-snapshot

Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins

What points at this work

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

inferred← citeshttps://doi.org/10.1016/j.celrep.2023.112037openalex-snapshot

The selective autophagy adaptor p62/SQSTM1 forms phase condensates regulated by HSP27 that facilitate the clearance of damaged lysosomes via lysophagy

inferred← citeshttps://doi.org/10.1038/s41598-021-92408-4openalex-snapshot

FIP200 controls the TBK1 activation threshold at SQSTM1/p62-positive condensates

inferred← citeshttps://doi.org/10.1083/jcb.202309145openalex-snapshot

AMPK regulates phagophore-to-autophagosome maturation

inferred← citeshttps://doi.org/10.1126/sciadv.abg4922openalex-snapshot

Reconstitution of cargo-induced LC3 lipidation in mammalian selective autophagy

inferred← citeshttps://doi.org/10.3389/fmicb.2022.1019543openalex-snapshot

The crucial role of the regulatory mechanism of the Atg1/ULK1 complex in fungi

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