Cited by 111RNA Research and SplicingCancer-related Molecular PathwaysProtein Kinase Regulation and GTPase Signaling

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A Role for Sam68 in Cell Cycle Progression Antagonized by a Spliced Variant within the KH Domain

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Barlat, Isabelle, Maurier, Florence, Duchesne, Marc, Guitard, Estelle, Tocque, Bruno, Schweighoffer, Fabien·1997·Journal of Biological Chemistry

DOI 10.1074/jbc.272.6.3129

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Abstract

Sam68 is the main tyrosine-phosphorylated and Src-associated protein in mitotic cells. Sam68 exhibits a conserved functional KH (hnRNPK homology) RNA binding domain and binds single strand nucleic acids. Tyrosine phosphorylation mediates the interaction of Sam68 with many SH3- and SH2-containing proteins and negatively regulates its nucleic acid binding properties. But the function and the impact of Sam68 on cell signaling and cell proliferation remains elusive. We report here the identification of a natural isoform of Sam68 with a deletion within the KH domain. This isoform, called Sam68DeltaKH, is specifically expressed at growth arrest upon confluency in normal cells. In cells that do not enter quiescence at confluency such as Src-transformed cells, no recruitment of Sam68DeltaKH is observed. Transfected Sam68DeltaKH inhibits serum-induced DNA synthesis and cyclin D1 expression. Sam68 overcomes these effects, suggesting that isoforms of Sam68 are involved, through KH domain signaling, in cell proliferation, and more precisely in G1/S transition.

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Retracted

Authors: Barlat, I., Maurier, F., Duchesne, M., Guitard, E., Tocque, B., & Schweighoffer, F.
Corresponding author: Schweighoffer, Fabien
ORCID: Maurier, Florence
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1997-02
Volume: 272
Issue: 6
Pages: 3129-3132
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.272.6.3129
OpenAlex: W2026506733
Cited by: 111
References: 22
Citations by year: 2024: 4 · 2023: 2 · 2021: 12 · 2019: 2 · 2018: 1 · 2016: 4 · 2015: 3 · 2013: 5 · 2012: 2
FWCI: 2.73
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8650 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: Sam68, KH domain, alternative splicing, protein isoforms, cell cycle progression, G1/S transition, cyclin D1, tyrosine phosphorylation, RNA binding, cell proliferation, quiescence, confluency, DNA synthesis
MeSH terms: Cell Cycle, DNA-Binding Proteins, Humans, Phosphoproteins, Phosphorylation, Structure-Activity Relationship, Transfection, Tyrosine, Polymerase Chain Reaction, S Phase, RNA-Binding Proteins, Adaptor Proteins, Signal Transducing

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A Role for Sam68 in Cell Cycle Progression Antagonized by a Spliced Variant within the KH Domain

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