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Regulation of SRF protein stability by an autophagy-dependent pathway
- Publication Year :
- 2019
-
Abstract
- Serum response factor (SRF), a key transcription factor, plays an important role in regulating cell functions such as proliferation and differentiation. Most proteins are unstable, and protein stability is regulated through the ubiquitin-proteasome system (UPS) or the autophagy lysosome pathway (ALP). Whether SRF is degraded and what mechanisms control SRF protein stability remain unexplored. Western blot analyses of cells treated with cycloheximide (CHX), a protein synthesis inhibitor, showed that SRF was degraded in a time-dependent manner. Moreover, we observed that SRF undergoes autophagy-dependent destruction, which is accelerated by serum deprivation. Through bioinformatics screening, we found that SRF contains the GSK3β phosphorylation motif (T/SPPXS): SPDSPPRSDPT, which is conserved from zebrafish to humans. Serum deprivation stimulated GSK3β activation that then potentiates SRF degradation through the autophagy lysosome pathway. Since SRF is important for numerous cellular activities, our results suggest that the autophagy-dependent SRF degradation pathway may provide a new avenue to modulate SRF-mediated cell functions.
- Subjects :
- 0301 basic medicine
Serum Response Factor
genetic structures
Biophysics
Cycloheximide
Biochemistry
Article
Culture Media, Serum-Free
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Western blot
Lysosome
Serum response factor
Chlorocebus aethiops
medicine
Autophagy
Animals
Humans
Molecular Biology
Zebrafish
Gene
Transcription factor
Cells, Cultured
Glycogen Synthase Kinase 3 beta
biology
medicine.diagnostic_test
Chemistry
Protein Stability
Cell Biology
biology.organism_classification
musculoskeletal system
eye diseases
Cell biology
Rats
030104 developmental biology
medicine.anatomical_structure
030220 oncology & carcinogenesis
embryonic structures
COS Cells
cardiovascular system
Lysosomes
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....986f7fd941724af71ba1c062a5e94224