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J Biol Chem, Vol. 273, Issue 30, 19183-19189, July 24, 1998
From the The transmembrane protein CD5, expressed on all T
cells and the B1 subset of B cells, modulates antigen receptor-mediated activation. We used the yeast two-hybrid system to identify proteins that interact with its cytoplasmic domain and play a role in CD5 proximal signaling events. We found that the
Regulation of Casein Kinase 2 by Direct Interaction with Cell
Surface Receptor CD5
,
,
,
, and
Division of Clinical Immunology and
Rheumatology, Department of Medicine, University of Alabama at
Birmingham, Birmingham, Alabama 35294 and the
Department of
Biochemistry, University of Western Ontario, London, Ontario
N6A 5C1, Canada
subunit of the serine/threonine kinase casein kinase 2 (CK2) interacts specifically with the cytoplasmic domain of CD5. Co-immunoprecipitation experiments showed activation-independent association of CK2 with CD5 in human and
murine B and T cell lines and murine splenocytes. The interaction of
CK2 holoenzyme with CD5 is mediated by the amino terminus of the
regulatory subunit
. CK2 binds and phosphorylates CD5 at the CK2
motifs flanked by Ser459 and Ser461.
Cross-linking of CD5 leads to the activation of CD5-associated CK2 in a
murine B-lymphoma cell line and a human T-leukemia cell line and is
independent of net recruitment of CK2 to CD5. In contrast, CK2 is not
activated following cross-linking of the B cell receptor complex or the
T cell receptor complex. This direct regulation of CK2 by a cell
surface receptor provides a novel pathway for control of cell
activation that could play a significant role in regulation of
CD5-dependent antigen receptor activation in T and B cells.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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