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Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function.

Malik M Keshwani¹, Brandon E Aubol¹, Laurent Fattet¹

¹*Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093-0636, U.S.A.

The Biochemical Journal

|December 23, 2014

Summary

This summary is machine-generated.

Specific serine-proline phosphorylation in SR proteins like SRSF1 alters their structure and function. This modification regulates alternative splicing for over 100 human genes, impacting gene expression programs.

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High-throughput Screening for Protein-based Inheritance in S. cerevisiae

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Published on: August 8, 2017

Area of Science:

Molecular Biology
Genetics
Biochemistry

Background:

Alternative splicing of human genes relies on SR proteins, characterized by arginine-serine rich (RS) domains.
SR proteins are phosphorylated by SR-specific protein kinases (SRPKs) and Cdc2-like kinases (CLKs).
The precise role of serine-proline phosphorylation by CLKs within RS domains remains unclear due to overlapping specificities with SRPKs.

Purpose of the Study:

To investigate the impact of serine-proline phosphorylation on the conformation and cellular function of the SR protein SRSF1.
To establish a direct link between specific chemical modifications in SR proteins and the regulation of alternative splicing.

Main Methods:

Utilized chemical tagging and dephosphorylation experiments to study SRSF1.
Analyzed changes in SRSF1 conformation and nuclear localization.
Assessed alterations in SRSF1 binding to exonic splicing enhancers.
Performed global splicing assays to evaluate effects on alternative splicing of human genes.

Main Results:

Serine-proline dipeptide modification significantly broadens the conformational ensemble of SRSF1.
Induced structural changes lead to SRSF1 mobilization within the nucleus.
Altered binding mechanisms of SRSF1 to exonic splicing enhancers in precursor mRNA were observed.
Global splicing assays revealed changes in alternative splicing for over 100 human genes.

Conclusions:

Specific serine-proline phosphorylation directly influences SRSF1 conformation and dynamics.
These conformational changes are critical for regulating SRSF1's interaction with mRNA and its function in splicing.
The study establishes a causal relationship between a specific post-translational modification in SR proteins and the regulation of alternative gene splicing programs.