ArticleJournal of molecular biology2011
Regulating SR protein phosphorylation through regions outside the kinase domain of SRPK1.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Review
- Computational analysis of regulatory regions in human protein kinases.Protein science : a publication of the Protein Society · 2023Article
- Functions of SRPK, CLK and DYRK kinases in stem cells, development, and human developmental disorders.FEBS letters · 2023Review
- Targeting pre-mRNA splicing in cancers: roles, inhibitors, and therapeutic opportunities.Frontiers in oncology · 2023Review
- Phosphorylation mediated regulation of RNA splicing in plants.Frontiers in plant science · 2023Review
- LIMK2 promotes the metastatic progression of triple-negative breast cancer by activating SRPK1.Oncogenesis · 2020Article
- Aberrant alternative splicing in breast cancer.Journal of molecular cell biology · 2019Review
- Redox-dependent gating of VDAC by mitoNEET.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Pharmacology of Modulators of Alternative Splicing.Pharmacological reviews · 2017Review
- Evidence for disulfide bonds in SR Protein Kinase 1 (SRPK1) that are required for activity and nuclear localization.PloS one · 2017Article
- N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation.The Biochemical journal · 2014Article
- Recruiting a silent partner for activation of the protein kinase SRPK1.Biochemistry · 2014Article
- SRPK2 phosphorylates tau and mediates the cognitive defects in Alzheimer's disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Nucleotide release sequences in the protein kinase SRPK1 accelerate substrate phosphorylation.Biochemistry · 2012Article
Corrections and comments
- Erratum issuedWhitehouse, Jennifer [corrected to Whitesides, Jennifer]
Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
SR proteins (splicing factors containing arginine-serine repeats) are essential splicing factors whose phosphorylation by the SR-specific protein kinase (SRPK) family regulates nuclear localization and mRNA processing activity. In addition to an N-terminal extension with unknown function, SRPKs contain a large, nonhomologous spacer insert domain (SID) that bifurcates the kinase domain and anchors the kinase in the cytoplasm through interactions with chaperones. While structures for the kinase domain are now available, constructs that include regions outside this domain have been resistant to crystallographic elucidation. To investigate the conformation of the full-length kinase and the functional role of noncatalytic regions, we performed hydrogen-deuterium exchange and steady-state kinetic experiments on SRPK1. Unlike the kinase core, the large SID lacks stable, hydrogen-bonded structure and may provide an intrinsically disordered region for chaperone interactions. Conversely, the N-terminus, which positively regulates SR protein binding, adopts a stable structure when the insert domain is present and stabilizes a docking groove in the large lobe of the kinase domain. The N-terminus and SID equally enhance SR protein turnover by altering the stability of several catalytic loop segments. These studies reveal that SRPK1 uses an N-terminal extension and a large, intrinsically disordered region juxtaposed to a stable structure to facilitate high-affinity SR protein interactions and phosphorylation rates.
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Registered trials
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.