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

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

Research output: Contribution to journalArticle

117 Citations (Scopus)

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 antiphosphotyrosine (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
StatePublished - Oct 1992
Externally publishedYes

Fingerprint

T-Cell Antigen Receptor
Tyrosine
Chemical activation
T-cells
Proteins
Yeast
Amino Acid Sequence
Complementary DNA
T-Lymphocytes
Amino Acids
Phosphorylation
Cloning
Cell Cycle Checkpoints
Mitosis
Protein-Tyrosine Kinases
Purification
Ligation
Sequence Analysis
Saccharomyces cerevisiae
Organism Cloning

Keywords

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

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Egerton, M., Ashe, O. R., Chen, D., Druker, B., Burgess, W. H., & Samelson, L. E. (1992). VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation. EMBO Journal, 11(10), 3533-3540.

VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation. / Egerton, M.; Ashe, O. R.; Chen, D.; Druker, Brian; Burgess, W. H.; Samelson, L. E.

In: EMBO Journal, Vol. 11, No. 10, 10.1992, p. 3533-3540.

Research output: Contribution to journalArticle

Egerton, M, Ashe, OR, Chen, D, Druker, B, Burgess, WH & Samelson, LE 1992, 'VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation', EMBO Journal, vol. 11, no. 10, pp. 3533-3540.
Egerton, M. ; Ashe, O. R. ; Chen, D. ; Druker, Brian ; Burgess, W. H. ; Samelson, L. E. / VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation. In: EMBO Journal. 1992 ; Vol. 11, No. 10. pp. 3533-3540.
@article{932490c507dc4e139a41af5af185d9d1,
title = "VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation",
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 antiphosphotyrosine (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.",
keywords = "Cell cycle, Phosphorylation, Signal transduction, T-lymphocyte",
author = "M. Egerton and Ashe, {O. R.} and D. Chen and Brian Druker and Burgess, {W. H.} and Samelson, {L. E.}",
year = "1992",
month = "10",
language = "English (US)",
volume = "11",
pages = "3533--3540",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "10",

}

TY - JOUR

T1 - VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation

AU - Egerton, M.

AU - Ashe, O. R.

AU - Chen, D.

AU - Druker, Brian

AU - Burgess, W. H.

AU - Samelson, L. E.

PY - 1992/10

Y1 - 1992/10

N2 - 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 antiphosphotyrosine (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.

AB - 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 antiphosphotyrosine (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.

KW - Cell cycle

KW - Phosphorylation

KW - Signal transduction

KW - T-lymphocyte

UR - http://www.scopus.com/inward/record.url?scp=0026660330&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026660330&partnerID=8YFLogxK

M3 - Article

VL - 11

SP - 3533

EP - 3540

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 10

ER -