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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 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 chain. We also demonstrate that assembly
of the CD3 subunits with cytoskeleton-associated 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 appears as a 21-kDa protein, phosphorylated
cytoskeleton-associated 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 are enhanced, while phosphorylated 16-kDa
cytoskeleton-associated exhibits little change; 2) soluble
non-phosphorylated 16-kDa translocates to the cytoskeleton; 3)
activation-dependent ubiquitinated 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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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.
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