PMID- 10564820
OWN - NLM
STAT- MEDLINE
DCOM- 20000111
LR  - 20190707
IS  - 0378-1119 (Print)
IS  - 0378-1119 (Linking)
VI  - 240
IP  - 1
DP  - 1999 Nov 15
TI  - Salpalpha and Salpbeta, growth-arresting homologs of Sam68.
PG  - 133-47
AB  - Sam68, a nuclear RNA-binding protein, is a major substrate of the Src tyrosine
      kinase in mitotic cells. In addition to a tyrosine-rich C-terminal region, Sam68 
      also has six poly-proline (SH3-binding) sites, many of which are located in an
      amino-terminal region. Sam68 appears to act as an adaptor protein, associating
      with many SH2- and SH3-containing signal-transducing proteins (Richard et al.,
      Mol. Cell. Biol. 15:186-197, 1995). Here we describe a novel 55kDa protein,
      Salpalpha, which has sequence similarity to Sam68 throughout its length.
      Salpalpha lacks the amino-terminal region found in Sam68, and has only a single
      poly-proline site, which binds the SH3 domain of the p85 subunit of PI 3-kinase. 
      Salpalpha is tyrosine-phosphorylated when expressed in Rous sarcoma
      virus-infected chicken embryo fibroblasts (RSV-CEF); unlike Sam68, however,
      Salpalpha does not co-precipitate with v-Src. Salpbeta, an alternatively spliced 
      isoform lacking the C-terminal tyrosine-rich region, is also
      tyrosine-phosphorylated in RSV-CEF, and also binds the SH3 domain of p85. We
      further show that expression of either Salpalpha or Salpbeta down-regulates the
      expression of Sam68 in CEF, and arrests the growth of these cells. Our results
      suggest that Salp may function as a negative regulator of cell growth.
FAU - Lee, J
AU  - Lee J
AD  - University of Texas at Dallas, Department of Molecular Biology, Richardson, TX,
      USA.
FAU - Burr, J G
AU  - Burr JG
LA  - eng
SI  - GENBANK/AF051321
SI  - GENBANK/AF051322
PT  - Journal Article
PL  - Netherlands
TA  - Gene
JT  - Gene
JID - 7706761
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (DNA, Complementary)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (KHDRBS1 protein, human)
RN  - 0 (KHDRBS3 protein, human)
RN  - 0 (Khdrbs1 protein, mouse)
RN  - 0 (Khdrbs3 protein, mouse)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Protein Isoforms)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA-Binding Proteins)
RN  - EC 2.7.1.- (Phosphatidylinositol 3-Kinases)
RN  - EC 2.7.10.2 (Oncogene Protein pp60(v-src))
SB  - IM
MH  - 3T3 Cells
MH  - Adaptor Proteins, Signal Transducing
MH  - Alternative Splicing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Blotting, Northern
MH  - Cell Division/*genetics
MH  - Chick Embryo
MH  - Chromosome Mapping
MH  - Chromosomes, Human, Pair 8/genetics
MH  - DNA, Complementary/chemistry/genetics
MH  - DNA-Binding Proteins
MH  - Down-Regulation
MH  - Female
MH  - Gene Expression Regulation
MH  - HeLa Cells
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/*genetics/metabolism
MH  - Oncogene Protein pp60(v-src)/metabolism
MH  - Phosphatidylinositol 3-Kinases/chemistry/metabolism
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Protein Isoforms/genetics/metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - RNA-Binding Proteins/*genetics/metabolism
MH  - Sequence Alignment
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
MH  - Tissue Distribution
MH  - src Homology Domains
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - S0378111999004217 [pii]
AID - 10.1016/s0378-1119(99)00421-7 [doi]
PST - ppublish
SO  - Gene. 1999 Nov 15;240(1):133-47. doi: 10.1016/s0378-1119(99)00421-7.