ArticleMolecular biology of the cell1997
Mss4 does not function as an exchange factor for Rab in endoplasmic reticulum to Golgi transport.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 55 citations in OpenAlex.
- A conformation-dependent hydrophobic degron determines Rab9a-mediated vesicular trafficking.The Journal of biological chemistry · 2026Article
- Protein quality control machinery supports primary ciliogenesis by eliminating GDP-bound Rab8-family GTPases.iScience · 2023Article
- Stratum is required for both apical and basolateral transport through stable expression of Rab10 and Rab35 inMolecular biology of the cell · 2022Article
- Structural Insights into the Regulation Mechanism of Small GTPases by GEFs.Molecules (Basel, Switzerland) · 2019Review
- Cytoplasmic control of Rab family small GTPases through BAG6.EMBO reports · 2019Article
- RABIF/MSS4 is a Rab-stabilizing holdase chaperone required for GLUT4 exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The G protein α chaperone Ric-8 as a potential therapeutic target.Molecular pharmacology · 2015Review
- The intraflagellar transport protein IFT27 promotes BBSome exit from cilia through the GTPase ARL6/BBS3.Developmental cell · 2014Article
- Mss4 protein is a regulator of stress response and apoptosis.Cell death & disease · 2012Article
- Histamine-releasing factor has a proinflammatory role in mouse models of asthma and allergy.The Journal of clinical investigation · 2012Article
- Role of Rab GTPases in membrane traffic and cell physiology.Physiological reviews · 2011Review
- Rab GEFs and GAPs.Current opinion in cell biology · 2010Review
- Structural mechanisms for regulation of membrane traffic by rab GTPases.Traffic (Copenhagen, Denmark) · 2009Review
- Characterization of TCTP, the translationally controlled tumor protein, from Arabidopsis thaliana.The Plant cell · 2008Article
- Structural basis for Rab GTPase activation by VPS9 domain exchange factors.Nature structural & molecular biology · 2007Article
- A catalytic coiled coil: structural insights into the activation of the Rab GTPase Sec4p by Sec2p.Molecular cell · 2007Article
- Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4.The EMBO journal · 2006Article
- Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.The EMBO journal · 2005Article
- Translationally controlled tumor protein acts as a guanine nucleotide dissociation inhibitor on the translation elongation factor eEF1A.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport.Molecular biology of the cell · 2002Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mss4 and its yeast homologue, Dss4, have been proposed to function as guanine nucleotide exchange factors (GEFs) for a subset of Rab proteins in the secretory pathway. We have previously shown that Rab1A mutants defective in GTP-binding potently inhibit endoplasmic reticulum to Golgi transport, presumably by sequestering an unknown GEF regulating its function. We now demonstrate that these mutants stably associate with Mss4 both in vivo and in vitro and that Mss4 effectively neutralizes the inhibitory activity of the Rab1A mutants. An equivalent Rab3A mutant (Rab3A[N135I]), a Rab protein specifically involved in regulated secretion at the cell surface, associates with Mss4 as efficiently as the Rab1A[N124I] mutant. Although Rab3A[N135I] prevents the ability of Mss4 to neutralize the inhibitory effects of Rab1A mutants on transport, it has no effect on Rab1 function or endoplasmic reticulum to Golgi transport. Furthermore, quantitative immunodepletion of Mss4 fails to inhibit transport in vitro. We conclude that Mss4 and its yeast homologue, Dss4, are not GEFs mediating activation of Rab, but rather, they interact with the transient guanine nucleotide-free state, defining a new class of Ras-superfamily GTPase effectors that function as guanine nucleotide-free chaperones (GFCs).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.