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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
Published on: August 9, 2019
pPKCδ activates SC35 splicing factor during H9c2 myoblastic differentiation
Susi Zara1, Mirella Falconi, Monica Rapino
1Department of Drug Sciences, Faculty of Pharmacy, University G d'Annunzio, Chieti-Pescara, Italy. s.zara@unich.it
Histology and Histopathology
|December 1, 2010
Summary
Phosphorylated Protein Kinase C delta (pPKCδ) interacts with splicing factor SC35 in the nucleus, activating transcription and influencing cardiomyoblast differentiation. This PKCδ-SC35 interaction is key to cardiac cell development.
Area of Science:
- Cell Biology
- Molecular Biology
- Cardiovascular Research
Background:
- Protein Kinase C (PKC) isoforms are crucial for cardiac development and aging.
- The nuclear interactions of PKC isoforms with specific substrates, like splicing factors, remain understudied.
Purpose of the Study:
- Investigate the expression, localization, and interaction of PKC isoforms (α, δ, ε, ζ) with splicing factor SC35.
- Determine the role of PKC isoforms in modulating the transcription machinery during cardiomyoblast differentiation.
Main Methods:
- Utilized H9c2 cells induced to myoblast differentiation.
- Employed western blotting, co-immunoprecipitation, and electron microscopy for analysis.
- Assessed expression, distribution, and interaction of PKC isoforms and SC35.
Main Results:
- PKCδ was the most expressed isoform in differentiated H9c2 cells.
- Phosphorylated PKCδ (pPKCδ) showed increased nuclear interaction and co-localization with SC35.
- No significant changes in PKCδ and SC35 distribution were observed between different serum conditions.
Conclusions:
- pPKCδ activation of SC35 suggests a direct role in modulating transcription via nuclear interaction.
- The pPKCδ-SC35 nuclear co-localization is critical for downstream transcriptional changes.
- This interaction influences morphological modifications associated with cardiomyoblast differentiation.
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