Tyrosine phosphorylation of alpha tubulin in human T lymphocytes

Ley, S. C., Verbi, W., Pappin, D. J., Druker, B., Davies, A. A., Crumpton, M. J. (January 1994) Tyrosine phosphorylation of alpha tubulin in human T lymphocytes. Eur J Immunol, 24 (1). pp. 99-106. ISSN 0014-2980 (Print)0014-2980 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/7517366
DOI: 10.1002/eji.1830240116

Abstract

N-terminal sequencing of the 55- and 50-kDa polypeptides affinity purified on a phosphotyrosine monoclonal antibody column from activated Jurkat T cells identified alpha and beta tubulin. Two-dimensional gel analysis indicated that alpha tubulin was directly phosphorylated on tyrosine. beta Tubulin was not detectably tyrosine phosphorylated but was precipitated by anti-phosphotyrosine (PTyr) antibody by virtue of its association with the alpha subunit as a heterodimer. Phosphotyrosyl alpha tubulin was not incorporated into intact microtubules and was all in the unpolymerized soluble fraction. These results suggest that tyrosine phosphorylation of alpha tubulin may inhibit the ability of this subunit to polymerize into microtubules. Stimulation of Jurkat T cells via T cell receptor increased the amount of tubulin precipitated by the anti-PTyr antibody. These data raise the possibility that the polymerization of tubulin heterodimers may be regulated by phosphorylation on tyrosine during T cell activation.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Electrophoresis, Gel, Two-Dimensional Humans Microtubules/ chemistry Molecular Sequence Data Phosphoproteins/ chemistry Phosphotyrosine Precipitin Tests T-Lymphocytes/ chemistry Tubulin/ chemistry Tumor Cells, Cultured Tyrosine/ analogs & derivatives/analysis
Subjects: organs, tissues, organelles, cell types and functions > cell types and functions > cell types > T cells
organs, tissues, organelles, cell types and functions > cell types and functions > cell types > T cells
organs, tissues, organelles, cell types and functions > cell types and functions > cell types > T cells

bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Matt Covey
Date: January 1994
Date Deposited: 09 Sep 2014 20:31
Last Modified: 09 Sep 2014 20:31
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30789

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