PMID- 10077576 OWN - NLM STAT- MEDLINE DCOM- 19990520 LR - 20190501 IS - 0027-8424 (Print) IS - 0027-8424 (Linking) VI - 96 IP - 6 DP - 1999 Mar 16 TI - Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosis. PG - 2710-5 AB - Sam68, the 68-kDa Src substrate associated during mitosis, is an RNA-binding protein with signaling properties that contains a GSG (GRP33, Sam68, GLD-1) domain. Here we report the cloning of two Sam68-like-mammalian proteins, SLM-1 and SLM-2. These proteins have an approximately 70% sequence identity with Sam68 in their GSG domain. SLM-1 and SLM-2 have the characteristic Sam68 SH2 and SH3 domain binding sites. SLM-1 is an RNA-binding protein that is tyrosine phosphorylated by Src during mitosis. SLM-1 bound the SH2 and SH3 domains of p59(fyn), Grb-2, phospholipase Cgamma-1 (PLCgamma-1), and/or p120(rasGAP), suggesting it may function as a multifunctional adapter protein for Src during mitosis. SLM-2 is an RNA-binding protein that is not tyrosine phosphorylated by Src or p59(fyn). Moreover, SLM-2 did not associate with the SH3 domains of p59(fyn), Grb-2, PLCgamma-1, or p120(rasGAP), suggesting that SLM-2 may not function as an adapter protein for these proteins. The identification of SLM-1 and SLM-2 demonstrates the presence of a Sam68/SLM family whose members have the potential to link signaling pathways with RNA metabolism. FAU - Di Fruscio, M AU - Di Fruscio M AD - Terry Fox Molecular Oncology Group, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, Department of Oncology, McGill University, Montreal, PQ H3T 1E2, Canada. FAU - Chen, T AU - Chen T FAU - Richard, S AU - Richard S LA - eng SI - GENBANK/AF098796 SI - GENBANK/AF099092 PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - United States TA - Proc Natl Acad Sci U S A JT - Proceedings of the National Academy of Sciences of the United States of America JID - 7505876 RN - 0 (Adaptor Proteins, Signal Transducing) RN - 0 (DNA-Binding Proteins) RN - 0 (KHDRBS1 protein, human) RN - 0 (KHDRBS2 protein, human) RN - 0 (KHDRBS3 protein, human) RN - 0 (Khdrbs1 protein, mouse) RN - 0 (Khdrbs2 protein, mouse) RN - 0 (Khdrbs3 protein, mouse) RN - 0 (RNA-Binding Proteins) RN - EC 2.7.10.2 (src-Family Kinases) SB - IM MH - Adaptor Proteins, Signal Transducing MH - Amino Acid Sequence MH - Animals MH - DNA-Binding Proteins MH - HeLa Cells MH - Humans MH - Mice MH - Mitosis/*genetics MH - Molecular Sequence Data MH - RNA-Binding Proteins/*genetics/metabolism MH - Sequence Alignment MH - Substrate Specificity MH - src-Family Kinases/*genetics/metabolism PMC - PMC15834 EDAT- 1999/03/17 00:00 MHDA- 1999/03/17 00:01 CRDT- 1999/03/17 00:00 PHST- 1999/03/17 00:00 [pubmed] PHST- 1999/03/17 00:01 [medline] PHST- 1999/03/17 00:00 [entrez] AID - 10.1073/pnas.96.6.2710 [doi] PST - ppublish SO - Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2710-5. doi: 10.1073/pnas.96.6.2710.