Abstract
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 Mr ~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 activation2. 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 fusion4,5, 26S proteasome function6, regulation of the expression of human immunodeficiency virus7,8, and assembly of peroxisomes9. 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.
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Pleasure, I., Black, M. & Keen, J. Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein. Nature 365, 459–462 (1993). https://doi.org/10.1038/365459a0
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DOI: https://doi.org/10.1038/365459a0
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