VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation

M. Egerton, O. R. Ashe, D. Chen, B. J. Druker, W. H. Burgess, L. E. Samelson

Research output: Contribution to journalArticle

120 Scopus citations

Abstract

Activation of T cells through the T cell antigen receptor (TCR) results in the rapid tyrosine phosphorylation of a number of cellular proteins, one of the earliest being a 100 kDa protein. We have sought to identify this 100 kDa substrate by partially purifying the protein by amtiphosphotyrosine (APT) affinity purification, in order to obtain amino acid sequence data and, using this information, to isolate the cDNA clone encoding the molecule. We report here that the amino acid sequence data showed pp100 to be the murine equivalent of porcine valosin containing protein (VCP), a finding confirmed from the cloning and sequencing of the murine pp100 cDNA. Sequence analysis has shown VCP to be a member of a family of ATP binding, homo-oligomeric proteins, and the mammalian homolog of Saccharomyces cerevisiae cdc48p, a protein essential to the completion of mitosis in yeast. We also provide proof that both endogenous and expressed murine VCP are tyrosine phosphorylated in response to T cell activation. Thus we have identified a novel component of the TCR mediated tyrosine kinase activation pathway that may provide a link between TCR ligation and cell cycle control.

Original languageEnglish (US)
Pages (from-to)3533-3540
Number of pages8
JournalEMBO Journal
Volume11
Issue number10
DOIs
StatePublished - 1992

Keywords

  • Cell cycle
  • Phosphorylation
  • Signal transduction
  • T-lyphocyte

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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