Cited by 99RNA Research and SplicingProtein Kinase Regulation and GTPase SignalingProtein Tyrosine Phosphatases

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

Open access
Di Fruscio, Marco, Chen, Taiping, Richard, Stéphane·1999·Proceedings of the National Academy of Sciences

Abstract

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.

Integrity signals

Registry

Crossref · 10.1073/pnas.96.6.2710

Cites

53 of 53 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • 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]

Cites

Flagged first, then by citations

Cited by

Sorted by citations

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
Published
1999-03-16
Volume
96
Issue
6
Pages
2710-2715
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
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
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review