Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosis
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Sam68, the 68-kDa S rc substrate a ssociated during m itosis, is an RNA-binding protein with signaling properties that contains a GSG ( G RP33, S am68, G LD-1) domain. Here we report the cloning of two S am68- l ike- m ammalian proteins, SLM-1 and SLM-2. These proteins have an ≈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 Cγ-1 (PLCγ-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, PLCγ-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.
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The KHDRBS family has three members: SAM68, SLM1 and SLM2.
“The KHDRBS family has three members: SRC-associated in mitosis 68 kDa protein (SAM68; also known as KHDRBS1), SLM1 (also known as KHDRBS2) and SLM2 (also known as KHDRBS3)80.”
From The neurogenetics of alternative splicing (2016) · cites this paper as [80]
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- Authors
- Di Fruscio, M., Chen, T., & Richard, S.
- Affiliations
- Terry Fox Molecular Oncology Group, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, and Departments of Oncology, Medicine, and Microbiology and Immunology, McGill University, Montréal, PQ H3T 1E2, Canada
- Jewish General Hospital (CA)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1999-03-16
- Volume
- 96
- Issue
- 6
- Pages
- 2710-2715
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC15834
- OpenAlex
- W2110112927
- Cited by
- 99
- References
- 53
- Citations by year
- 2026: 1 · 2025: 4 · 2022: 1 · 2021: 1 · 2019: 1 · 2018: 3 · 2017: 1 · 2016: 6 · 2015: 3 · 2014: 4 · 2013: 6 · 2012: 3
- FWCI
- 2.53
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- Sam68, RNA-binding proteins, Src kinase, mitosis, adaptor proteins, SH2 and SH3 domains, Fyn, Grb2, p120RasGAP, tyrosine phosphorylation, RNA metabolism, signaling pathways
- MeSH terms
- Amino Acid Sequence, Animals, DNA-Binding Proteins, HeLa Cells, Humans, Mitosis, Molecular Sequence Data, Substrate Specificity, Sequence Alignment, RNA-Binding Proteins, src-Family Kinases, Adaptor Proteins, Signal Transducing, Mice
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