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.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Alternative Splicing*
-
Animals
-
Cell Line
-
Cells, Cultured
-
Dopamine and cAMP-Regulated Phosphoprotein 32 / antagonists & inhibitors
-
Dopamine and cAMP-Regulated Phosphoprotein 32 / genetics
-
Dopamine and cAMP-Regulated Phosphoprotein 32 / metabolism*
-
Exons
-
Humans
-
In Vitro Techniques
-
Models, Biological
-
Nerve Tissue Proteins / metabolism*
-
Neurons / metabolism
-
Protein Binding
-
Protein Phosphatase 1 / metabolism
-
RNA Precursors / genetics
-
RNA Precursors / metabolism
-
RNA Processing, Post-Transcriptional
-
RNA, Small Interfering / genetics
-
RNA-Binding Proteins / metabolism*
-
Rats
-
Serine-Arginine Splicing Factors
-
Signal Transduction
Substances
-
Dopamine and cAMP-Regulated Phosphoprotein 32
-
Nerve Tissue Proteins
-
PPP1R1B protein, human
-
RNA Precursors
-
RNA, Small Interfering
-
RNA-Binding Proteins
-
TRA2B protein, human
-
Serine-Arginine Splicing Factors
-
Protein Phosphatase 1