ArticleThe EMBO journal2006
Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
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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
49 citing papers in PubMed, 103 citations in OpenAlex.
- AS160 is a lipid-responsive regulator of cardiac CaNature communications · 2024Article
- 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
- ADP-Ribosylation Factor Family of Small GTP-Binding Proteins: Their Membrane Recruitment, Activation, Crosstalk and Functions.Frontiers in cell and developmental biology · 2022Review
- Impact of C-terminal truncations in the Arabidopsis Rab escort protein (REP) on REP-Rab interaction and plant fertility.The Plant journal : for cell and molecular biology · 2021Article
- Guanine nucleotide exchange factors activate Rab8a for Toll-like receptor signalling.Small GTPases · 2021Article
- 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
- GEF mechanism revealed by the structure of SmgGDS-558 and farnesylated RhoA complex and its implication for a chaperone mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural determinants of Rab11 activation by the guanine nucleotide exchange factor SH3BP5.Nature communications · 2018Article
- Molecular control of Rab activity by GEFs, GAPs and GDI.Small GTPases · 2018Review
- Rab GTPases and their interacting protein partners: Structural insights into Rab functional diversity.Small GTPases · 2018Review
- Article
- SCD1 and SCD2 Form a Complex That Functions with the Exocyst and RabE1 in Exocytosis and Cytokinesis.The Plant cell · 2017Article
- 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
- Timing and Reset Mechanism of GTP Hydrolysis-Driven Conformational Changes of Atlastin.Structure (London, England : 1993) · 2017Article
- Stratum, a Homolog of the Human GEF Mss4, Partnered with Rab8, Controls the Basal Restriction of Basement Membrane Proteins in Epithelial Cells.Cell reports · 2017Article
- A modification switch on a molecular switch: Phosphoregulation of Rab7 during endosome maturation.Small GTPases · 2016Article
- A pull-down procedure for the identification of unknown GEFs for small GTPases.Small GTPases · 2016Article
- New insights into the molecular mechanism of the Rab GTPase Sec4p activation.BMC structural biology · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rab GTPases function as essential regulators of vesicle transport in eukaryotic cells. MSS4 was shown to stimulate nucleotide exchange on Rab proteins associated with the exocytic pathway and to have nucleotide-free-Rab chaperone activity. A detailed kinetic analysis of MSS4 interaction with Rab8 showed that MSS4 is a relatively slow exchange factor that forms a long-lived nucleotide-free complex with RabGTPase. In contrast to other characterized exchange factor-GTPase complexes, MSS4:Rab8 complex binds GTP faster than GDP, but still ca. 3 orders of magnitude more slowly than comparable complexes. The crystal structure of the nucleotide-free MSS4:Rab8 complex revealed that MSS4 binds to the Switch I and interswitch regions of Rab8, forming an intermolecular beta-sheet. Complex formation results in dramatic structural changes of the Rab8 molecule, leading to unfolding of the nucleotide-binding site and surrounding structural elements, facilitating nucleotide release and slowing its rebinding. Coupling of nucleotide exchange activity to a cycle of GTPase unfolding and refolding represents a novel nucleotide exchange mechanism.
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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.