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Cited by 316

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The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C.

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Yao, L, Kawakami, Y, Kawakami, T·1994·Proceedings of the National Academy of Sciences

Abstract

Bruton tyrosine kinase (EC 2.7.1.112) [Btk, encoded by Btk in mice and BTK in humans (formerly known as atk, BPK, or emb)], which is variously mutated in chromosome X-linked agammaglobulinemia patients and X-linked immunodeficient (xid) mice, has the pleckstrin homology (PH) domain at its amino terminus. The PH domain of Btk expressed as a bacterial fusion protein directly interacts with protein kinase C in mast cell lysates. Evidence was obtained that Btk is physically associated with protein kinase C in intact murine mast cells as well. Both Ca(2+)-dependent (alpha, beta I, and beta II) and Ca(2+)-independent protein kinase C isoforms (epsilon and zeta) in mast cells interact with the PH domain of Btk in vitro, and protein kinase C beta I is associated with Btk in vivo. Btk served as a substrate of protein kinase C, and its enzymatic activity was down-regulated by protein kinase C-mediated phosphorylation. Furthermore, depletion or inhibition of protein kinase C with pharmacological agents resulted in an enhancement of the tyrosine phosphorylation of Btk induced by mast cell activation.

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Metadata

Authors
Yao, L., Kawakami, Y., & Kawakami, T.
Venue
Proceedings of the National Academy of Sciences
Published
1994-09-13
Volume
91
Issue
19
Pages
9175-9179
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2041121472
Cited by
316
References
0
FWCI
14.49
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C. https://app.cochat.ai/papers/10.1073/pnas.91.19.9175
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Yao, L., Kawakami, Y., & Kawakami, T. (1994). The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.19.9175

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