Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis.

Stenmark, H.; Parton, R.G.; Steele‐Mortimer, O.; Lütcke, A.; Gruenberg, J.; Zerial, M.

doi:10.1002/j.1460-2075.1994.tb06381.x

Cited by 968Cellular transport and secretionProtein Kinase Regulation and GTPase SignalingAutophagy in Disease and Therapy

Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis.

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Stenmark, H., Parton, R.G., Steele‐Mortimer, O., Lütcke, A., Gruenberg, J., Zerial, M.·1994·The EMBO Journal

DOI 10.1002/j.1460-2075.1994.tb06381.xPMC PMC394944

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Abstract

Small GTPases of the rab family control distinct steps of intracellular transport. The function of their GTPase activity is not completely understood. To investigate the role of the nucleotide state of rab5 in the early endocytic pathway, the effects of two mutants with opposing biochemical properties were tested. The Q79L mutant of rab5, analogous with the activating Q61L mutant of p21-ras, was found to have a strongly decreased intrinsic GTPase activity and was, unlike wild-type rab5, found mainly in the GTP-bound form in vivo. Expression of this protein in BHK and HeLa cells led to a dramatic change in cell morphology, with the appearance of unusually large early endocytic structures, considerably larger than those formed upon overexpression of wild-type rab5. An increased rate of transferrin internalization was observed in these cells, whereas recycling was inhibited. Cytosol containing rab5 Q79L stimulated homotypic early endosome fusion in vitro, even though it contained only a small amount of the isoprenylated protein. A different mutant, rab5 S34N, was found, like the inhibitory p21-ras S17N mutant, to have a preferential affinity for GDP. Overexpression of rab5 S34N induced the accumulation of very small endocytic profile and inhibited transferrin endocytosis. This protein inhibited fusion between early endosomes in vitro. The opposite effects of the rab5 Q79L and S34N mutants suggest that rab5:GTP is required prior to membrane fusion, whereas GTP hydrolysis by rab5 occurs after membrane fusion and functions to inactivate the protein.

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The lumen of these endosomes contains the ILVs.
“The lumen of these endosomes contains the ILVs. 46”
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Authors: Stenmark, H., Parton, R. G., Steele‐Mortimer, O., Lütcke, A., Gruenberg, J., & Zerial, M.
Affiliations: European Molecular Biology Laboratory (DE)
ORCID: Stenmark, H.
Parton, R.G.
Steele‐Mortimer, O.
Gruenberg, J.
Zerial, M.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1994-03-01
Volume: 13
Issue: 6
Pages: 1287-1296
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1994.tb06381.x
PMC: PMC394944
OpenAlex: W1606338704
Cited by: 968
References: 72
Citations by year: 2026: 19 · 2025: 20 · 2024: 34 · 2023: 18 · 2022: 18 · 2021: 24 · 2020: 20 · 2019: 19 · 2018: 30 · 2017: 30 · 2016: 30 · 2015: 36 · 2014: 40 · 2013: 41 · 2012: 42
FWCI: 9.26
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Norges Forskningsråd
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords: Rab5, GTPase activity, early endosomes, membrane fusion, endocytosis, GTP-bound state, GDP-bound state, transferrin internalization, endosome recycling, intracellular transport, small GTPases
MeSH terms: Animals, Base Sequence, Cells, Cultured, Cytosol, Endocytosis, Cricetinae, HeLa Cells, Humans, Membrane Fusion, Microscopy, Electron, Microscopy, Fluorescence, Molecular Sequence Data, Transferrin, Protein Prenylation, DNA Primers, GTP-Binding Proteins, GTP Phosphohydrolases, rab5 GTP-Binding Proteins

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Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis.

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