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Rhomboid intramembrane protease RHBDL4 triggers ER-export and non-canonical secretion of membrane-anchored TGFα
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/0471143030.cb0322s30openalex-snapshot
Isolation and Characterization of Exosomes from Cell Culture Supernatants and Biological Fluids
inferredcites →https://doi.org/10.1002/jcb.21923openalex-snapshot
Secretion of active membrane type 1 matrix metalloproteinase (MMP‐14) into extracellular space in microvesicular exosomes
inferredcites →https://doi.org/10.1016/0378-1119(89)90358-2openalex-snapshot
Site-directed mutagenesis by overlap extension using the polymerase chain reaction
inferredcites →https://doi.org/10.1016/j.bbrc.2004.03.039openalex-snapshot
Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2
inferredcites →https://doi.org/10.1016/j.ceb.2014.05.004openalex-snapshot
Biogenesis and secretion of exosomes
inferredcites →https://doi.org/10.1016/j.cell.2011.02.047openalex-snapshot
Rhomboid Family Pseudoproteases Use the ER Quality Control Machinery to Regulate Intercellular Signaling
inferredcites →https://doi.org/10.1016/j.cub.2004.01.025openalex-snapshot
Diverse Substrate Recognition Mechanisms for Rhomboids Thrombomodulin Is Cleaved by Mammalian Rhomboids
inferredcites →https://doi.org/10.1016/j.cub.2011.03.043openalex-snapshot
Amphiregulin Exosomes Increase Cancer Cell Invasion
inferredcites →https://doi.org/10.1016/j.febslet.2013.04.033openalex-snapshot
Rhomboid domain containing 1 inhibits cell apoptosis by upregulating AP‐1 activity and its downstream target Bcl‐3
inferredcites →https://doi.org/10.1016/j.mce.2010.04.008openalex-snapshot
EGF receptor activation by GPCRs: An universal pathway reveals different versions
inferredcites →https://doi.org/10.1016/j.molcel.2006.01.034openalex-snapshot
Role for CED-9 and Egl-1 as Regulators of Mitochondrial Fission and Fusion Dynamics
inferredcites →https://doi.org/10.1016/j.molcel.2009.11.006openalex-snapshot
Sequence-Specific Intramembrane Proteolysis: Identification of a Recognition Motif in Rhomboid Substrates
inferredcites →https://doi.org/10.1016/j.molcel.2012.06.008openalex-snapshot
Ubiquitin-Dependent Intramembrane Rhomboid Protease Promotes ERAD of Membrane Proteins
inferredcites →https://doi.org/10.1016/j.molcel.2014.10.012openalex-snapshot
The Yeast ER-Intramembrane Protease Ypf1 Refines Nutrient Sensing by Regulating Transporter Abundance
inferredcites →https://doi.org/10.1016/j.semcdb.2014.03.003openalex-snapshot
From wavy hair to naked proteins: The role of transforming growth factor alpha in health and disease
inferredcites →https://doi.org/10.1016/j.tcb.2015.07.003openalex-snapshot
Clipping or Extracting: Two Ways to Membrane Protein Degradation
inferredcites →https://doi.org/10.1016/j.yexcr.2008.10.011openalex-snapshot
The role of protease activity in ErbB biology
inferredcites →https://doi.org/10.1016/s0021-9258(18)35940-4openalex-snapshot
Cleavage of membrane-anchored growth factors involves distinct protease activities regulated through common mechanisms.
inferredcites →https://doi.org/10.1016/s0092-8674(01)00525-6openalex-snapshot
Drosophila Rhomboid-1 Defines a Family of Putative Intramembrane Serine Proteases
inferredcites →https://doi.org/10.1016/s0092-8674(01)00526-8openalex-snapshot
Regulated Intracellular Ligand Transport and Proteolysis Control EGF Signal Activation in Drosophila
inferredcites →https://doi.org/10.1016/s0092-8674(05)80064-9openalex-snapshot
The cytoplasmic carboxy-terminal amino acid specifies cleavage of membrane TGFα into soluble growth factor
inferredcites →https://doi.org/10.1016/s1097-2765(03)00181-3openalex-snapshot
Substrate Specificity of Rhomboid Intramembrane Proteases Is Governed by Helix-Breaking Residues in the Substrate Transmembrane Domain
inferredcites →https://doi.org/10.1038/47260openalex-snapshot
EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
inferredcites →https://doi.org/10.1038/embor.2011.50openalex-snapshot
Mammalian EGF receptor activation by the rhomboid protease RHBDL2
inferredcites →https://doi.org/10.1038/embor.2013.128openalex-snapshot
Mammalian iRhoms have distinct physiological functions including an essential role in TACE regulation
inferredcites →https://doi.org/10.1038/nature14357openalex-snapshot
Cytosolic extensions directly regulate a rhomboid protease by modulating substrate gating
inferredcites →https://doi.org/10.1038/ncb2510openalex-snapshot
Genome-wide RNAi screening identifies human proteins with a regulatory function in the early secretory pathway
inferredcites →https://doi.org/10.1038/ncomms9022openalex-snapshot
Rhomboid domain containing 1 promotes colorectal cancer growth through activation of the EGFR signalling pathway
inferredcites →https://doi.org/10.1038/nm1275openalex-snapshot
Angiotensin II and EGF receptor cross-talk in chronic kidney diseases: a new therapeutic approach
inferredcites →https://doi.org/10.1038/nrd3320openalex-snapshot
G protein-coupled receptors: novel targets for drug discovery in cancer
inferredcites →https://doi.org/10.1038/sj.emboj.7601581openalex-snapshot
Rhomboid cleaves Star to regulate the levels of secreted Spitz
inferredcites →https://doi.org/10.1038/sj.onc.1200848openalex-snapshot
Bcl-2, Bcl-xL and adenovirus protein E1B19kD are functionally equivalent in their ability to inhibit cell death
inferredcites →https://doi.org/10.1038/sj.onc.1208614openalex-snapshot
SCF-mediated protein degradation and cell cycle control
inferredcites →https://doi.org/10.1042/bj20051013openalex-snapshot
A role for exosomes in the constitutive and stimulus-induced ectodomain cleavage of L1 and CD44
inferredcites →https://doi.org/10.1073/pnas.1505649112openalex-snapshot
iRhoms 1 and 2 are essential upstream regulators of ADAM17-dependent EGFR signaling
inferredcites →https://doi.org/10.1074/jbc.271.19.11376openalex-snapshot
Diverse Cell Surface Protein Ectodomains Are Shed by a System Sensitive to Metalloprotease Inhibitors
inferredcites →https://doi.org/10.1074/jbc.m111.251983openalex-snapshot
RNF170 Protein, an Endoplasmic Reticulum Membrane Ubiquitin Ligase, Mediates Inositol 1,4,5-Trisphosphate Receptor Ubiquitination and Degradation
inferredcites →https://doi.org/10.1074/jbc.m401453200openalex-snapshot
Metalloproteinase-dependent Transforming Growth Factor-α Release Mediates Neurotensin-stimulated MAP Kinase Activation in Human Colonic Epithelial Cells
inferredcites →https://doi.org/10.1074/mcp.m700342-mcp200openalex-snapshot
A Versatile Nanotrap for Biochemical and Functional Studies with Fluorescent Fusion Proteins
inferredcites →https://doi.org/10.1083/jcb.121.6.1299openalex-snapshot
The cytoplasmic tail of CD44 is required for basolateral localization in epithelial MDCK cells but does not mediate association with the detergent-insoluble cytoskeleton of fibroblasts.
inferredcites →https://doi.org/10.1083/jcb.200912082openalex-snapshot
MAPK signaling to the early secretory pathway revealed by kinase/phosphatase functional screening
inferredcites →https://doi.org/10.1091/mbc.8.8.1619openalex-snapshot
The carboxyl-terminal valine residues of proTGF alpha are required for its efficient maturation and intracellular routing.
inferredcites →https://doi.org/10.1091/mbc.e05-02-0155openalex-snapshot
Golgi Inheritance in Mammalian Cells Is Mediated through Endoplasmic Reticulum Export Activities
inferredcites →https://doi.org/10.1091/mbc.e06-01-0014openalex-snapshot
Substrate Selectivity of Epidermal Growth Factor-Receptor Ligand Sheddases and their Regulation by Phorbol Esters and Calcium Influx
inferredcites →https://doi.org/10.1093/emboj/cdg111openalex-snapshot
TACE is required for the activation of the EGFR by TGF‐α in tumors
inferredcites →https://doi.org/10.1093/jnci/82.5.402openalex-snapshot
High-Density Functional Gastrin Releasing Peptide Receptors on Primate Cells
inferredcites →https://doi.org/10.1093/nar/30.2.e9openalex-snapshot
High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
inferredcites →https://doi.org/10.1096/fj.08-112771openalex-snapshot
Human rhomboid family‐1 gene RHBDF1 participates in GPCR‐mediated transactivation of EGFR growth signals in head and neck squamous cancer cells
inferredcites →https://doi.org/10.1101/gad.14.13.1651openalex-snapshot
A family of rhomboid-like genes: Drosophila rhomboid-1 and roughoid/rhomboid-3 cooperate to activate EGF receptor signaling
inferredcites →https://doi.org/10.1101/gad.4.2.190openalex-snapshot
rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster.
inferredcites →https://doi.org/10.1101/gr.6425307openalex-snapshot
Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases
inferredcites →https://doi.org/10.1111/j.1349-7006.2006.00278.xopenalex-snapshot
Sivelestat, a specific neutrophil elastase inhibitor, suppresses the growth of gastric carcinoma cells by preventing the release of transforming growth factor‐α
inferredcites →https://doi.org/10.1111/j.1471-4159.2011.07253.xopenalex-snapshot
The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking
inferredcites →https://doi.org/10.1111/j.1600-0854.2011.01219.xopenalex-snapshot
Intramembrane Proteolysis in Regulated Protein Trafficking
inferredcites →https://doi.org/10.1126/science.1214400openalex-snapshot
Tumor Necrosis Factor Signaling Requires iRhom2 to Promote Trafficking and Activation of TACE
inferredcites →https://doi.org/10.1126/science.1214448openalex-snapshot
iRhom2 Regulation of TACE Controls TNF-Mediated Protection Against Listeria and Responses to LPS
inferredcites →https://doi.org/10.1126/science.282.5392.1281openalex-snapshot
An Essential Role for Ectodomain Shedding in Mammalian Development
inferredcites →https://doi.org/10.1146/annurev-cellbio-100913-012944openalex-snapshot
The Rhomboid-Like Superfamily: Molecular Mechanisms and Biological Roles
inferredcites →https://doi.org/10.1158/0008-5472.can-13-1027openalex-snapshot
Human Rhomboid Family-1 Suppresses Oxygen-Independent Degradation of Hypoxia-Inducible Factor-1α in Breast Cancer
inferredcites →https://doi.org/10.1242/dev.126.12.2663openalex-snapshot
rhomboid and Star interact synergistically to promote EGFR/MAPK signaling during Drosophila wing vein development
inferredcites →https://doi.org/10.1371/journal.pbio.0020334openalex-snapshot
EGF Signal Propagation during C. elegans Vulval Development Mediated by ROM-1 Rhomboid
inferredcites →https://doi.org/10.1371/journal.pone.0037452openalex-snapshot
Exosome-Related Multi-Pass Transmembrane Protein TSAP6 Is a Target of Rhomboid Protease RHBDD1-Induced Proteolysis
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4798512openalex-extracted
Extensive Targeting of Chemical Space at the Prime Side of Ketoamide Inhibitors of Rhomboid Proteases by Branched Substituents Empowers Their Selectivity and Potency
inferred← citeshttps://doi.org/10.1002/jcp.70094openalex-snapshot
Holding Out for a Model: Rhomboid Superfamily in Vertebrate Development and Disease
inferred← citeshttps://doi.org/10.1007/s00018-026-06377-wopenalex-snapshot
Rhomboid protease RHBDL2 is a calcium-activated suppressor of EGFR signalling in keratinocytes
inferred← citeshttps://doi.org/10.1016/b978-0-12-818168-3.00012-7openalex-snapshot
Rhomboid proteases leading to cancer: Structures, functions, and inhibition
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2017.04.016openalex-snapshot
Rhomboid proteases in human disease: Mechanisms and future prospects
inferred← citeshttps://doi.org/10.1016/j.celrep.2022.111175openalex-snapshot
Rhomboid protease RHBDL4 promotes retrotranslocation of aggregation-prone proteins for degradation
inferred← citeshttps://doi.org/10.1016/j.ebiom.2018.09.038openalex-snapshot
Human rhomboid family-1 modulates clathrin coated vesicle-dependent pro-transforming growth factor α membrane trafficking to promote breast cancer progression
inferred← citeshttps://doi.org/10.1016/j.ejmech.2024.116606openalex-snapshot
Extensive targeting of chemical space at the prime side of ketoamide inhibitors of rhomboid proteases by branched substituents empowers their selectivity and potency
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.101935openalex-snapshot
The mammalian rhomboid protein RHBDL4 protects against endoplasmic reticulum stress by regulating the morphology and distribution of ER sheets
inferred← citeshttps://doi.org/10.1016/j.jbc.2024.107541openalex-snapshot
Eta-secretase-like processing of the amyloid precursor protein (APP) by the rhomboid protease RHBDL4
inferred← citeshttps://doi.org/10.1016/j.semcdb.2016.06.022openalex-snapshot
Inactive rhomboid proteins: New mechanisms with implications in health and disease
inferred← citeshttps://doi.org/10.1016/j.semcdb.2016.07.033openalex-snapshot
Substrates and physiological functions of secretase rhomboid proteases
inferred← citeshttps://doi.org/10.1016/j.semcdb.2016.08.021openalex-snapshot
Rhomboid protease inhibitors: Emerging tools and future therapeutics
inferred← citeshttps://doi.org/10.1021/acs.biochem.2c00680openalex-snapshot
Putative Protein Interactome of the Rhomboid Protease RHBDL4
inferred← citeshttps://doi.org/10.1021/acs.chemrev.5c00780openalex-snapshot
Navigating Misfolded Terrain: ER-Associated Degradation of Membrane Proteins
inferred← citeshttps://doi.org/10.1021/acschembio.9b00404openalex-snapshot
Discovery of Cellular Roles of Intramembrane Proteases
inferred← citeshttps://doi.org/10.1021/acsomega.0c06030openalex-snapshot
Compartmentalized Proteomic Profiling Outlines the Crucial Role of the Classical Secretory Pathway during Recombinant Protein Production in Chinese Hamster Ovary Cells
inferred← citeshttps://doi.org/10.1038/s41467-024-45615-2openalex-snapshot
RHBDL4-triggered downregulation of COPII adaptor protein TMED7 suppresses TLR4-mediated inflammatory signaling
inferred← citeshttps://doi.org/10.1038/s41467-025-67697-2openalex-snapshot
Rhomboid protease GlpG regulates type 1 pili quality control and virulence in pathogenic E. coli
inferred← citeshttps://doi.org/10.1038/s41586-022-04414-9openalex-snapshot
Mechanism-based traps enable protease and hydrolase substrate discovery
inferred← citeshttps://doi.org/10.1038/s41598-017-07556-3openalex-snapshot
Quantitative proteomics screen identifies a substrate repertoire of rhomboid protease RHBDL2 in human cells and implicates it in epithelial homeostasis
inferred← citeshttps://doi.org/10.1038/s41598-023-48769-zopenalex-snapshot
The generation of detergent-insoluble clipped fragments from an ERAD substrate in mammalian cells
inferred← citeshttps://doi.org/10.1042/bcj20160783openalex-snapshot
The AAA+ ATPase p97, a cellular multitool
inferred← citeshttps://doi.org/10.1042/bcj20190022openalex-snapshot
The DCBLD receptor family: emerging signaling roles in development, homeostasis and disease
inferred← citeshttps://doi.org/10.1074/jbc.m116.753582openalex-snapshot
Alternative Processing of the Amyloid Precursor Protein Family by Rhomboid Protease RHBDL4
inferred← citeshttps://doi.org/10.1074/jbc.ra118.002640openalex-snapshot
Membrane cholesterol as regulator of human rhomboid protease RHBDL4
inferred← citeshttps://doi.org/10.1074/jbc.ra118.005642openalex-snapshot
The intramembrane protease SPP impacts morphology of the endoplasmic reticulum by triggering degradation of morphogenic proteins
inferred← citeshttps://doi.org/10.1074/jbc.ra118.007074openalex-snapshot
Spatial proteomics reveal that the protein phosphatase PTP1B interacts with and may modify tyrosine phosphorylation of the rhomboid protease RHBDL4
inferred← citeshttps://doi.org/10.1083/jcb.202602106openalex-snapshot
Rhomboid protease Rhbdl2 influences macrophage recruitment and wound repair in zebrafish
inferred← citeshttps://doi.org/10.1093/pnasnexus/pgad351openalex-snapshot
Rhomboid protease RHBDL4/RHBDD1 cleaves SREBP-1c at endoplasmic reticulum monitoring and regulating fatty acids
inferred← citeshttps://doi.org/10.1096/fj.202002087ropenalex-snapshot
Interleukin‐11 (IL‐11) receptor cleavage by the rhomboid protease RHBDL2 induces IL‐11 trans‐signaling
inferred← citeshttps://doi.org/10.1101/2021.06.15.448480openalex-snapshot
RHBDL4 protects against endoplasmic reticulum stress by regulating the morphology and distribution of ER sheets
inferred← citeshttps://doi.org/10.1101/2021.08.24.457590openalex-snapshot
Rhomboid protease RHBDL4/RHBDD1 cleaves SREBP-1c at ER monitoring and regulating fatty acids
inferred← citeshttps://doi.org/10.1101/2023.09.04.555897openalex-snapshot
Eta-secretase-like processing of the amyloid precursor protein (APP) by RHBDL4
inferred← citeshttps://doi.org/10.1101/2025.09.09.675128openalex-snapshot
Mechanistic insight into the regulation of virulence factor type 1 pili in pathogenic E. coli by rhomboid protease GlpG
inferred← citeshttps://doi.org/10.1111/febs.13979openalex-snapshot
Intramembrane proteases as drug targets
inferred← citeshttps://doi.org/10.1111/jne.12690openalex-snapshot
Tanycytes: A rich morphological history to underpin future molecular and physiological investigations
inferred← citeshttps://doi.org/10.1186/s12964-018-0267-5openalex-snapshot
Rhomboid domain-containing protein 1 promotes breast cancer progression by regulating the p-Akt and CDK2 levels
inferred← citeshttps://doi.org/10.1186/s13046-018-0687-5openalex-snapshot
RHBDD1 promotes colorectal cancer metastasis through the Wnt signaling pathway and its downstream target ZEB1
inferred← citeshttps://doi.org/10.1186/s40001-025-03116-yopenalex-snapshot
RHBDD1 induces cell cycle arrest in TP53-mutant NSCLC cells by promoting endoplasmic reticulum-associated degradation of p53 and DNA-PKcs
inferred← citeshttps://doi.org/10.1242/jcs.217745openalex-snapshot
Intramembrane proteolysis at a glance: from signalling to protein degradation
inferred← citeshttps://doi.org/10.1242/jcs.243790openalex-snapshot
Intramembrane protease RHBDL4 cleaves oligosaccharyltransferase subunits to target them for ER-associated degradation
inferred← citeshttps://doi.org/10.1242/jcs.264719openalex-snapshot
A Golgi-bypass secretion mechanism for proTGFα involving TMED9 and GRASP65
inferred← citeshttps://doi.org/10.1515/hsz-2018-0259openalex-snapshot
An alternative processing pathway of APP reveals two distinct cleavage modes for rhomboid protease RHBDL4
inferred← citeshttps://doi.org/10.2174/1386207325666220609120001openalex-snapshot
Prognostic and Immunological Significance of Rhomboid Domain Containing Protein 1 in Multiple Primary Cancers
inferred← citeshttps://doi.org/10.3390/biology15010057openalex-snapshot
Systematic Identification of the Serine Protease Family (StSPs) and Functional Characterization of the Secretory Protein StSP8-4 for Pathogenicity in Setosphaeria turcica
inferred← citeshttps://doi.org/10.3390/ijms20235958openalex-snapshot
Rhomboid-Like-2 Intramembrane Protease Mediates Metalloprotease-Independent Regulation of Cadherins
inferred← citeshttps://doi.org/10.3390/ijms22052514openalex-snapshot
The Tumor Proteolytic Landscape: A Challenging Frontier in Cancer Diagnosis and Therapy
inferred← citeshttps://doi.org/10.3390/ijms22094969openalex-snapshot
ADAM10 Site-Dependent Biology: Keeping Control of a Pervasive Protease
inferred← citeshttps://doi.org/10.3390/plants9030307openalex-snapshot
Arabidopsis RanBP2-Type Zinc Finger Proteins Related to Chloroplast RNA Editing Factor OZ1
inferred← citeshttps://doi.org/10.4149/neo_2021_210804n1107openalex-snapshot
Rhomboid domain containing 1 promotes the growth of non-small cell lung cancer through the activation of EGFR and regulation of the BIK-mediated apoptosis
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