PMID- 10498607
OWN - NLM
STAT- MEDLINE
DCOM- 19991104
LR  - 20181201
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 94
IP  - 7
DP  - 1999 Oct 1
TI  - Identification of the SH2 domain binding protein of Bruton's tyrosine kinase as
      BLNK--functional significance of Btk-SH2 domain in B-cell antigen
      receptor-coupled calcium signaling.
PG  - 2357-64
AB  - Bruton's tyrosine kinase (Btk) is a critical component in the B-cell antigen
      receptor (BCR)-coupled signaling pathway. Its deficiency in B cells leads to loss
      or marked reduction in the BCR-induced calcium signaling. It is known that this
      BCR-induced calcium signaling depends on the activation of phospholipase Cgamma
      (PLCgamma), which is mediated by Btk and another tyrosine kinase Syk and that the
      SH2 and pleckstrin homology (PH) domains of Btk play important roles in this
      activation process. Although the importance of the PH domain of Btk has been
      explained by its role in the membrane targeting of Btk, the functional
      significance of the SH2 domain in the calcium signaling has remained merely a
      matter of speculation. In this report, we identify that one of the major Btk-SH2 
      domain-binding proteins in B cells is BLNK (B-cell linker protein) and present
      evidences that the interaction of BLNK and the SH2 domain of Btk contributes to
      the complete tyrosine phosphorylation of PLCgamma.
FAU - Hashimoto, S
AU  - Hashimoto S
AD  - Department of Molecular Medicine, Osaka University Medical School, Osaka, Japan.
FAU - Iwamatsu, A
AU  - Iwamatsu A
FAU - Ishiai, M
AU  - Ishiai M
FAU - Okawa, K
AU  - Okawa K
FAU - Yamadori, T
AU  - Yamadori T
FAU - Matsushita, M
AU  - Matsushita M
FAU - Baba, Y
AU  - Baba Y
FAU - Kishimoto, T
AU  - Kishimoto T
FAU - Kurosaki, T
AU  - Kurosaki T
FAU - Tsukada, S
AU  - Tsukada S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Enzyme Precursors)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Isoenzymes)
RN  - 0 (Peptide Fragments)
RN  - 0 (Receptors, Antigen, T-Cell)
RN  - 0 (Recombinant Fusion Proteins)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (Agammaglobulinaemia Tyrosine Kinase)
RN  - EC 2.7.10.2 (BTK protein, human)
RN  - EC 2.7.10.2 (SYK protein, human)
RN  - EC 2.7.10.2 (Syk Kinase)
RN  - EC 3.1.4.- (Type C Phospholipases)
RN  - EC 3.1.4.3 (Phospholipase C gamma)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.50 (lysyl endopeptidase)
RN  - SY7Q814VUP (Calcium)
SB  - AIM
SB  - IM
MH  - Agammaglobulinaemia Tyrosine Kinase
MH  - Amino Acid Sequence
MH  - Amino Acid Substitution
MH  - Burkitt Lymphoma
MH  - Calcium/*physiology
MH  - Enzyme Precursors/metabolism
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Isoenzymes/metabolism
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Peptide Fragments/chemistry
MH  - Phospholipase C gamma
MH  - Protein-Tyrosine Kinases/*chemistry/*metabolism
MH  - Receptors, Antigen, T-Cell/*immunology
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Serine Endopeptidases
MH  - Signal Transduction
MH  - Syk Kinase
MH  - Transfection
MH  - Tumor Cells, Cultured
MH  - Type C Phospholipases/metabolism
MH  - src Homology Domains
EDAT- 1999/09/25 00:00
MHDA- 1999/09/25 00:01
CRDT- 1999/09/25 00:00
PHST- 1999/09/25 00:00 [pubmed]
PHST- 1999/09/25 00:01 [medline]
PHST- 1999/09/25 00:00 [entrez]
PST - ppublish
SO  - Blood. 1999 Oct 1;94(7):2357-64.