Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein

CLATHRIN is the structural protein of coated membranes involved in receptor-mediated endocytosis and aspects of Golgi sorting in eukaryotic cells. We have now detected a stoichiometric complex of clathrin with a novel protein of M r ~100,000 (100K) in lysates of different mammalian cells. Formation...

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Bibliographic Details
Published in:Nature (London) 1993-09, Vol.365 (6445), p.459-462
Main Authors: Pleasure, Irene T, Black, Mark M, Keen, James H
Format: Article
Language:English
Subjects:
3T3 Cells
Adenosine Triphosphatases
AIDS/HIV
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Biochemistry
Biological and medical sciences
Biological Transport
Cell Cycle Proteins
Cell Line
Clathrin - metabolism
Fundamental and applied biological sciences. Psychology
Fungal Proteins - chemistry
Heat-Shock Proteins - metabolism
Humanities and Social Sciences
Humans
letter
Mammalia
Mammals
Mice
Mice, Inbred BALB C
Miscellaneous
Molecular Sequence Data
multidisciplinary
Neurons - metabolism
Precipitin Tests
Protein Binding
Proteins
Rats
Science
Science (multidisciplinary)
Sympathetic Nervous System - cytology
Sympathetic Nervous System - metabolism
Transport processes
Valosin Containing Protein
Yeasts
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Summary:CLATHRIN is the structural protein of coated membranes involved in receptor-mediated endocytosis and aspects of Golgi sorting in eukaryotic cells. We have now detected a stoichiometric complex of clathrin with a novel protein of M r ~100,000 (100K) in lysates of different mammalian cells. Formation of the complex, which also includes the 70K heat-shock protein HscTO, occurs within 15 min of synthesis. The 100K protein has been identified as valosin-containing protein (VCP; ref. 1), an early substrate for tyrosine phosphorylation on T-cell receptor activation 2 . Further, VCP is the mammalian homologue of yeast Cdc48p (ref. 3) and is a member of a larger gene family that includes putative ATP-binding proteins involved in vesicle transport and fusion 4,5 , 26S proteasome function 6 , regulation of the expression of human immunodeficiency virus 7,8 , and assembly of peroxisomes 9 . The association with clathrin and the morphological and catalytic similarity to the chaperonin proteins indicate that VCP may modulate protein-protein interactions in membrane transport processes.
ISSN:0028-0836
1476-4687
DOI:10.1038/365459a0