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Science 7 January 1994:
Vol. 263. no. 5143, pp. 84 - 87
DOI: 10.1126/science.8272870
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Articles

Science, Vol 263, Issue 5143, 84-87
Copyright © 1994 by American Association for the Advancement of Science

articles

Location of cAMP-dependent protein kinase type I with the TCR-CD3 complex

BS Skalhegg, K Tasken, V Hansson, HS Huitfeldt, T Jahnsen, and T Lea

Institute of Medical Biochemistry, University of Oslo, Blindern, Norway.

Selective activation of cyclic adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase type I (cAKI), but not type II, is sufficient to mediate inhibition of T cell replication induced through the antigen-specific T cell receptor-CD3 (TCR-CD3) complex. Immunocytochemistry and immunoprecipitation studies of the molecular mechanism by which cAKI inhibits TCR-CD3-dependent T cell replication demonstrated that regulatory subunit I alpha, along with its associated kinase activity, translocated to and interacted with the TCR-CD3 complex during T cell activation and capping. Regulatory subunit II alpha did not. When stimulated by cAMP, the cAKI localized to the TCR-CD3 complex may release kinase activity that, through phosphorylation, might uncouple the TCR-CD3 complex from intracellular signaling systems.


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