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Stathmin phosphorylation patterns discriminate between distinct transduction pathways of human T lymphocyte activation through CD2 triggering
Author(s) -
le Gouvello Sabine,
Chneiweiss Herve,
Tarantino Nadine,
Debre Patrice,
Sobel Andre
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80020-4
Subject(s) - stathmin , phosphorylation , protein kinase c , microbiology and biotechnology , phosphoprotein , second messenger system , signal transduction , kinase , biology , phosphorylation cascade , intracellular , protein kinase a , protein phosphorylation , chemistry
CD2 triggering of human T lymphocyte activation has been associated with the activation of different interacting protein kinases, including protein kinase C (PKC). However the precise roles of its phosphorylated substrates are still unknown. We show here that PKC‐dependent and ‐independent pathways arc responsible for the CD2‐induced phosphorylation of stathmin, a ubiquitous soluble phosphoprotein, most likely acting as a general intracellular relay integrating various second messenger pathways. The phosphorylated variants of stathmin provide a fingerprint reflecting the second messenger pathway(s) stimulated. The respective roles of both PKC and stathmin in the regulation of T lymphocyte proliferation are discussed.