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PMID: 10077576 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosis.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 96 ·No. 6 ·1999-03-16 ·Pages 2710-5

Di Fruscio M, Chen T, Richard S

Abstract

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.

MeSH Terms
Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals DNA-Binding Proteins HeLa Cells Humans Mice Mitosis/genetics Molecular Sequence Data RNA-Binding Proteins/genetics,metabolism Sequence Alignment Substrate Specificity src-Family Kinases/genetics,metabolism
Chemicals
Adaptor Proteins, Signal Transducing DNA-Binding Proteins KHDRBS1 protein, human KHDRBS2 protein, human KHDRBS3 protein, human Khdrbs1 protein, mouse Khdrbs2 protein, mouse Khdrbs3 protein, mouse RNA-Binding Proteins src-Family Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Di Fruscio M
Terry Fox Molecular Oncology Group, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, Department of Oncology, McGill University, Montréal, PQ H3T 1E2, Canada.
Chen T
Richard S
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.96.6.2710
Published
1999-03-16
Pages
2710-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC15834
Subset
IM
Databases
GENBANK
AF098796, AF099092
External Links
PubMed source DOI: 10.1073/pnas.96.6.2710 PMC Full Text View journal details
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