Interactions of rab5 with cytosolic proteins

Kurzchalia, Teymuras V., Gorvel, Jean-Pierre, Dupree, Paul, Parton, Robert, Kellner, Roland, Houthaeve, Tony, Gruenberg, Jean and Simons, Kai (1992) Interactions of rab5 with cytosolic proteins. Journal of Biological Chemistry, 267 26: 18419-18423.

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Author Kurzchalia, Teymuras V.
Gorvel, Jean-Pierre
Dupree, Paul
Parton, Robert
Kellner, Roland
Houthaeve, Tony
Gruenberg, Jean
Simons, Kai
Title Interactions of rab5 with cytosolic proteins
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 1992-09-15
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 267
Issue 26
Start page 18419
End page 18423
Total pages 5
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
Rab proteins, one of the subfamilies of ras-like small GTP-binding proteins, are attached to cellular compartments or transport vesicles and may determine the specificity of fusion between these compartments and vesicles. It has been proposed that they alternate between a membrane-bound and a cytosolic state during their functional cycle. We have used a photo-cross- linking approach to identify their cytosolic interaction partners. In vitro synthesized rab5 was cross-linked in the presence of ATP mainly to three cytosolic proteins of 52, 65, and 85 kDa. Sucrose density gradient centrifugation of the cross-linked products suggested that they were part of a 10-14 S complex. Furthermore, rab5 was cross-linked to these and additional cytosolic proteins of 42, 48, and 160 kDa in the absence of ATP. Unexpectedly, upon ATP depletion of the cytosol cross-linked and noncross- linked rab5 was found in a sedimentable high molecular weight structure. Other members of the rab subfamily, but not N-ras, also sedimented under these conditions. Electrophoretic and electron microscopic analysis of the pelleted material revealed that it contained actin filament bundles and intermediate filaments. Our data suggest that cytosolic rab proteins interact with several proteins in a 10-14 S complex, and that the rab proteins may interact directly or indirectly via this complex with the cytoskeleton.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
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