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Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling.

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.

Pubmed ID: 7682714

Authors

  • Yamanashi Y
  • Okada M
  • Semba T
  • Yamori T
  • Umemori H
  • Tsunasawa S
  • Toyoshima K
  • Kitamura D
  • Watanabe T
  • Yamamoto T

Journal

Proceedings of the National Academy of Sciences of the United States of America

Publication Data

April 15, 1993

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Antibodies
  • Antibodies, Monoclonal
  • Antigens, CD45
  • B-Lymphocytes
  • Blood Proteins
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Immunoblotting
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments
  • Phosphoproteins
  • Phosphotyrosine
  • Protein-Tyrosine Kinases
  • Receptors, Antigen, T-Cell
  • Signal Transduction
  • Tumor Cells, Cultured
  • Tyrosine