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Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion.
- Source :
-
Cell [Cell] 1995 Nov 03; Vol. 83 (3), pp. 423-32. - Publication Year :
- 1995
-
Abstract
- We have identified a novel 100 kDa coiled-coil protein, rabaptin-5, that specifically interacts with the GTP form of the small GTPase Rab5, a potent regulator of endocytic transport. It is mainly cytosolic, but a fraction colocalizes with Rab5 to early endosomes. Expression of a GTPase-deficient Rab5 mutant enhances the binding of rabaptin-5 to enlarged endosomes. Overexpression of rabaptin-5 alone is sufficient to promote expansion of early endosomes. Rab5 recruits rabaptin-5 to purified early endosomes in a GTP-dependent manner, demonstrating functional similarities with other members of the Ras superfamily. Immunodepletion of rabaptin-5 from cytosol strongly inhibits Rab5-dependent early endosome fusion. Rabaptin-5 is thus a Rab effector required for membrane docking and fusion.
- Subjects :
- Amino Acid Sequence
Base Sequence
Cell-Free System
Cytosol chemistry
DNA, Complementary genetics
Endosomes physiology
Fungal Proteins physiology
Gene Expression physiology
Gene Library
Genetic Testing
Intracellular Membranes chemistry
Intracellular Membranes physiology
Membrane Proteins analysis
Molecular Sequence Data
Protein Binding physiology
Protein Structure, Secondary
Yeasts physiology
rab5 GTP-Binding Proteins
Endocytosis physiology
GTP Phosphohydrolases physiology
GTP-Binding Proteins physiology
Membrane Fusion physiology
Membrane Proteins physiology
Vesicular Transport Proteins
Subjects
Details
- Language :
- English
- ISSN :
- 0092-8674
- Volume :
- 83
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Cell
- Publication Type :
- Academic Journal
- Accession number :
- 8521472
- Full Text :
- https://doi.org/10.1016/0092-8674(95)90120-5