Open AccessIdentification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling.
Author(s) -
Yuji Yamanashi,
Masato Okada,
Toshihiko Semba,
Takashi Yamori,
Hisashi Umemori,
Susumu Tsunasawa,
Kumao Toyoshima,
Daisuke Kitamura,
Takeshi Watanabe,
Tadashi Yamamoto
Publication year - 1993
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.90.8.3631
Subject(s) - lyn , proto oncogene tyrosine protein kinase src , tyrosine protein kinase csk , receptor tyrosine kinase , biology , protein tyrosine phosphatase , tyrosine phosphorylation , tyrosine kinase , sh2 domain , sh3 domain , microbiology and biotechnology , ror1 , biochemistry , signal transduction , platelet derived growth factor receptor , receptor , growth factor
Crosslinking of membrane-bound immunoglobulins, which are B-cell antigen receptors, causes proliferation and differentiation of B cells or inhibition of their growth. The receptor-mediated signaling involves tyrosine phosphorylation of cellular proteins and rapid activation of Src-like kinases. The amino acid sequences of five proteolytic peptides of p75, a major substrate of protein-tyrosine(s) in the signaling, showed that p75 is the human HS1 gene product. The HS1 gene is expressed specifically in hematopoietic cells and encodes p75HS1, which carries both helix-turn-helix and Src homology 3 motifs. p75HS1 showed rapid tyrosine phosphorylation and association with a Src-like kinase, Lyn, after crosslinking of membrane-bound IgM. Thus, p75HS1 may be an important substrate of Lyn and possibly other protein-tyrosine kinases upon B-cell antigen receptor-mediated signaling.