DARPP-32 binds to tra2-beta1 and influences alternative splicing
Benderska, Natalya Becker, Kristina Girault, Jean-Antoine Becker, Cord-Michael Andreadis, Athena Stamm, Stefan
Benderska, Natalya
Becker, Kristina
Girault, Jean-Antoine
Becker, Cord-Michael
Andreadis, Athena
Stamm, Stefan
Citations
Altmetric:
Student Authors
Faculty Advisor
Academic Program
UMass Chan Affiliations
Document Type
Journal Article
Publication Date
2010-01-16
Keywords
*Alternative Splicing
Animals
Cell Line
Cells, Cultured
Dopamine and cAMP-Regulated Phosphoprotein 32
inhibitors
Exons
Humans
Models, Biological
Nerve Tissue Proteins
Neurons
Protein Binding
Protein Phosphatase 1
RNA Precursors
RNA Processing, Post-Transcriptional
RNA, Small Interfering
RNA-Binding Proteins
Rats
Signal Transduction
Cell Biology
Animals
Cell Line
Cells, Cultured
Dopamine and cAMP-Regulated Phosphoprotein 32
inhibitors
Exons
Humans
Models, Biological
Nerve Tissue Proteins
Neurons
Protein Binding
Protein Phosphatase 1
RNA Precursors
RNA Processing, Post-Transcriptional
RNA, Small Interfering
RNA-Binding Proteins
Rats
Signal Transduction
Cell Biology
Subject Area
Embargo Expiration Date
Link to Full Text
Abstract
The majority of human genes undergo alternative splicing, which is frequently altered in response to physiological stimuli. DARPP-32 (dopamine and cAMP regulated phosphoprotein, 32kDa) is a component of PKA-dependent signaling pathways. Here we show that DARPP-32 binds directly to the splicing factor tra2-beta1 (transformer 2). DARPP-32 changes the usage of tra2-beta1 dependent alternative exons in a concentration-dependent manner, suggesting that the DARPP-32:tra2-beta1 interaction is a molecular link between signaling pathways and pre-mRNA processing.
Source
Biochim Biophys Acta. 2010 May-Jun;1799(5-6):448-53. Epub 2010 Jan 13. Link to article on publisher's site
Year of Medical School at Time of Visit
Sponsors
Dates of Travel
DOI
10.1016/j.bbagrm.2010.01.003
Permanent Link to this Item
PubMed ID
20074680