Format

Send to

Choose Destination
Mol Biol Cell. 2016 Jan 15;27(2):410-20. doi: 10.1091/mbc.E15-09-0624. Epub 2015 Nov 12.

Sequential posttranslational modifications regulate PKC degradation.

Author information

1
Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Institute of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
2
Center for Translational Medicine, Shanghai Chest Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
3
Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL 32306.
4
Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Institute of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China liyong68@shsmu.edu.cn.

Abstract

Cross-talk among different types of posttranslational modifications (PTMs) has emerged as an important regulatory mechanism for protein function. Here we elucidate a mechanism that controls PKCα stability via a sequential cascade of PTMs. We demonstrate that PKCα dephosphorylation decreases its sumoylation, which in turn promotes its ubiquitination and ultimately enhances its degradation via the ubiquitin-proteasome pathway. These findings provide a molecular explanation for the activation-induced down-regulation of PKC proteins.

PMID:
26564794
PMCID:
PMC4713141
DOI:
10.1091/mbc.E15-09-0624
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Atypon Icon for PubMed Central
Loading ...
Support Center