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Volume 271, Number 34, Issue of August 23, 1996 pp. 20705-20712
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Normal T Cells Express Two T Cell Antigen Receptor Populations, One of Which Is Linked to the Cytoskeleton via zeta  Chain and Displays a Unique Activation-dependent Phosphorylation Pattern

(Received for publication, March 5, 1996)

Steve Caplan and Michal Baniyash

From The Lautenberg Center for General and Tumor Immunology, Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel

The TCR couples antigen recognition and the transmission of activation signals. We report the expression of two TCR populations on the surface of T lymphocytes, one of which is linked to the cytoskeleton via the zeta  chain. We also demonstrate that assembly of the CD3 subunits with cytoskeleton-associated zeta  is necessary for their maximal localization to the cytoskeleton. The potential significance of these two receptor forms is underscored by differences observed in non-activated T cells; while detergent-soluble phosphorylated zeta  appears as a 21-kDa protein, phosphorylated cytoskeleton-associated zeta  appears as a 16-kDa form. This dichotomous phosphorylation pattern is rigidly maintained following activation, although each of the receptor populations undergoes different activation-dependent modifications: 1) levels of soluble phosphorylated 21-kDa zeta  are enhanced, while phosphorylated 16-kDa cytoskeleton-associated zeta  exhibits little change; 2) soluble non-phosphorylated 16-kDa zeta  translocates to the cytoskeleton; 3) activation-dependent ubiquitinated zeta  forms localize to both fractions, albeit with different kinetics. We also show that the protein tyrosine kinase Lck undergoes activation-dependent modifications and translocates to the cytoskeleton. The phosphorylation profiles of the dichotomous TCR populations in both non-activated and activated lymphocytes suggest that each population could regulate distinct cellular functions, possibly by select intermolecular associations.


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