Evidence map›Paper›PMID 26167880›Full record

ArticleNature structural & molecular biology2015

SR protein kinases promote splicing of nonconsensus introns.

Jesse J Lipp, Michael C Marvin, Kevan M Shokat, Christine Guthrie

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 44 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Jesse J LippDepartment of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, California, USA.
Michael C MarvinDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California, USA.
Kevan M ShokatDepartment of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, California, USA.
Christine GuthrieDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California, USA.
Howard Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

BIOSYNTHESIS OF RNASR01GM021119 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GUTHRIE, CHRISTINE · 1985 to 2015
$12.9M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
DESIGNING SELECTIVE INHIBITORS OF CALCIUM-DEPENDENT KINASES IN PARASITESR01AI094098 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 2012 to 2015
$1.6M
Roles of S. pombe SR proteins in spliceosome function and assemblyF32GM101764 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MARVIN, MICHAEL CHARLES · 2012 to 2014
$156k
NCI NIH HHS CA-0052023NIAID NIH HHS R01 AI094098NIAID NIH HHS R01AI094098NIGMS NIH HHS 8P41GM103481NIGMS NIH HHS F32GM101764NIGMS NIH HHS R01 GM021119NIGMS NIH HHS R01GM021119
6 · The paper itself

Abstract

Phosphorylation of the spliceosome is essential for RNA splicing, yet how and to what extent kinase signaling affects splicing have not been defined on a genome-wide basis. Using a chemical genetic approach, we show in Schizosaccharomyces pombe that the SR protein kinase Dsk1 is required for efficient splicing of introns with suboptimal splice sites. Systematic substrate mapping in fission yeast and human cells revealed that SRPKs target evolutionarily conserved spliceosomal proteins, including the branchpoint-binding protein Bpb1 (SF1 in humans), by using an RXXSP consensus motif for substrate recognition. Phosphorylation of SF1 increases SF1 binding to introns with nonconsensus splice sites in vitro, and mutation of such sites to consensus relieves the requirement for Dsk1 and phosphorylated Bpb1 in vivo. Modulation of splicing efficiency through kinase signaling pathways may allow tuning of gene expression in response to environmental and developmental cues.

Indexed as

RNA SplicingAmino Acid MotifsAmino Acid SequenceBlotting, WesternIntronsMutationOligonucleotide Array Sequence AnalysisPhosphorylationProtein Serine-Threonine KinasesReverse Transcriptase Polymerase Chain ReactionRibonucleoprotein, U4-U6 Small NuclearRNA Splice SitesRNA Splicing FactorsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSubstrate SpecificityDsk1 protein kinaseProtein Serine-Threonine Kinasesprp4 protein, S pombeRibonucleoprotein, U4-U6 Small NuclearRNA Splice SitesRNA Splicing FactorsSchizosaccharomyces pombe Proteins

Identifiers

PMID26167880
OpenAlexW2204166508

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.