ArticleThe Journal of biological chemistry2010
Structural basis for homodimerization of the Src-associated during mitosis, 68-kDa protein (Sam68) Qua1 domain.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 43 citations in OpenAlex.
- Chemical Ligation of Backbone N-hydroxylated Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Hypoxia-Induced circPRELID2 Promotes Gastric Cancer Metastasis by Facilitating ZEB2 Translation via PCBP1 O-GlcNAcylation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Structure and function analysis of Sam68 and hnRNP A1 synergy in the exclusion of exon 7 from SMN2 transcripts.Protein science : a publication of the Protein Society · 2023Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- ITSN1 regulates SAM68 solubility through SH3 domain interactions with SAM68 proline-rich motifs.Cellular and molecular life sciences : CMLS · 2021Article
- SAM68 interaction with U1A modulates U1 snRNP recruitment and regulates mTor pre-mRNA splicing.Nucleic acids research · 2019Article
- Sequence, Structure, and Context Preferences of Human RNA Binding Proteins.Molecular cell · 2018Article
- Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.Nature communications · 2016Article
- Analysis of the interaction between host factor Sam68 and viral elements during foot-and-mouth disease virus infections.Virology journal · 2015Article
- The RNA-binding protein Sam68 regulates expression and transcription function of the androgen receptor splice variant AR-V7.Scientific reports · 2015Article
- Intrinsically disordered proteins in the nucleus of human cells.Biochemistry and biophysics reports · 2015Article
- SAM68: Signal Transduction and RNA Metabolism in Human Cancer.BioMed research international · 2015Review
- Evolutionary Dynamics of GLD-1-mRNA complexes in Caenorhabditis nematodes.Genome biology and evolution · 2014Article
- Structural and functional implications of the QUA2 domain on RNA recognition by GLD-1.Nucleic acids research · 2014Article
- Neuronal cell type-specific alternative splicing is regulated by the KH domain protein SLM1.The Journal of cell biology · 2014Article
- Screening protein--single stranded RNA complexes by NMR spectroscopy for structure determination.Methods (San Diego, Calif.) · 2014Article
- Role of Sam68 in post-transcriptional gene regulation.International journal of molecular sciences · 2013Review
- Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes.Chemphyschem : a European journal of chemical physics and physical chemistry · 2013Review
- Structure-function studies of STAR family Quaking proteins bound to their in vivo RNA target sites.Genes & development · 2013Article
- Alternative splicing programs in prostate cancer.International journal of cell biology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sam68 (Src-associated during mitosis, 68 kDa) is a prototypical member of the STAR (signal transducer and activator of RNA) family of RNA-binding proteins. STAR proteins bind mRNA targets and modulate cellular processes such as cell cycle regulation and tissue development in response to extracellular signals. Sam68 has been shown to modulate alternative splicing of the pre-mRNAs of CD44 and Bcl-xL, which are linked to tumor progression and apoptosis. Sam68 and other STAR proteins recognize bipartite RNA sequences and are thought to function as homodimers. However, the structural and functional roles of the self-association are not known. Here, we present the solution structure of the Sam68 Qua1 homodimerization domain. Each monomer consists of two antiparallel alpha-helices connected by a short loop. The two subunits are arranged perpendicular to each other in an unusual four-helix topology. Mutational analysis of Sam68 in vitro and in a cell-based assay revealed that the Qua1 domain and residues within the dimerization interface are essential for alternative splicing of a CD44 minigene. Together, our results indicate that the Qua1 homodimerization domain is required for regulation of alternative splicing by Sam68.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.