PMID- 10405761
OWN - NLM
STAT- MEDLINE
DCOM- 19990927
LR  - 20190921
IS  - 0898-6568 (Print)
IS  - 0898-6568 (Linking)
VI  - 11
IP  - 7
DP  - 1999 Jul
TI  - Tyrosine phosphorylation enhances the SH2 domain-binding activity of Bcr and
      inhibits Bcr interaction with 14-3-3 proteins.
PG  - 507-14
AB  - The cellular Bcr protein consists of an N-terminal serine/threonine kinase
      domain, a central guanine nucleotide exchange factor homology region and a
      C-terminal GTPase-activating protein domain. Previous work in our laboratory
      established that Bcr is a major transformation-related substrate for the v-Fps
      tyrosine kinase, and tyrosine phosphorylation of Bcr induces Bcr-Grb-2/SOS
      association in vivo through the Src homology 2 (SH2) domain of Grb-2. In the
      present study, we mapped the region of Bcr tyrosine phosphorylation by c-Fes, the
      human homologue of v-Fps, to Bcr N-terminal amino acids 162-413 by using a
      baculovirus/Sf-9 cell co-expression system. Tyrosine phosphorylation of Bcr by
      Fes greatly enhanced the binding of Bcr to the SH2 domains of multiple signalling
      molecules in vitro, including Grb-2, Ras GTPase activating protein, phospholipase
      C-gamma, the 85,000 M(r) subunit of phosphatidylinositol 3'-kinase, and the Abl
      tyrosine kinase. In contrast with SH2 binding, tyrosine phosphorylation of Bcr
      reduced its ability to associate with the 14-3-3 protein Bap-1 (Bcr-associated
      protein-1), a Bcr substrate and member of a family of phosphoserine-binding
      adaptor proteins. These experiments provide in vitro evidence that tyrosine
      phosphorylation may modulate the interaction of Bcr with multiple
      growth-regulatory signalling pathways.
FAU - Peters, K L
AU  - Peters KL
AD  - Eppley Institute for Research in Cancer, University of Nebraska Medical Center,
      Omaha 68198, USA.
FAU - Smithgall, T E
AU  - Smithgall TE
LA  - eng
GR  - CA58667/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Cell Signal
JT  - Cellular signalling
JID - 8904683
RN  - 0 (14-3-3 Proteins)
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (GRB2 Adaptor Protein)
RN  - 0 (GRB2 protein, human)
RN  - 0 (Proteins)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 42HK56048U (Tyrosine)
RN  - EC 1.14.16.2 (Tyrosine 3-Monooxygenase)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (FES protein, human)
RN  - EC 2.7.10.2 (Proto-Oncogene Proteins c-fes)
RN  - EC 2.7.10.2 (Proto-Oncogene Proteins pp60(c-src))
RN  - EC 2.7.11.1 (BCR protein, human)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (Proto-Oncogene Proteins c-bcr)
SB  - IM
MH  - 14-3-3 Proteins
MH  - *Adaptor Proteins, Signal Transducing
MH  - Cell Line
MH  - GRB2 Adaptor Protein
MH  - Humans
MH  - Phosphorylation
MH  - Protein-Serine-Threonine Kinases/genetics/*metabolism
MH  - Protein-Tyrosine Kinases/genetics/metabolism
MH  - Proteins/*metabolism
MH  - Proto-Oncogene Proteins/genetics/*metabolism
MH  - Proto-Oncogene Proteins c-bcr
MH  - Proto-Oncogene Proteins c-fes
MH  - Proto-Oncogene Proteins pp60(c-src)/metabolism
MH  - Tyrosine/*metabolism
MH  - *Tyrosine 3-Monooxygenase
MH  - *src Homology Domains
EDAT- 1999/07/16 00:00
MHDA- 1999/07/16 00:01
CRDT- 1999/07/16 00:00
PHST- 1999/07/16 00:00 [pubmed]
PHST- 1999/07/16 00:01 [medline]
PHST- 1999/07/16 00:00 [entrez]
AID - S0898-6568(99)00021-2 [pii]
AID - 10.1016/s0898-6568(99)00021-2 [doi]
PST - ppublish
SO  - Cell Signal. 1999 Jul;11(7):507-14. doi: 10.1016/s0898-6568(99)00021-2.