Affiliation:
1. Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, Illinois, USA
Abstract
Although an F-box protein, Mdm30, is found to regulate ubiquitylation of the Sub2 component of TREX (
tr
anscription-
ex
port) complex for proteasomal degradation in stimulation of mRNA export, it remains unknown whether such ubiquitin-proteasome system (UPS) regulation of Sub2 occurs cotranscriptionally via its interaction with Mdm30. Further, it is unclear whether impaired UPS regulation of Sub2 in the absence of Mdm30 alters mRNA export via splicing defects of export factors and/or mitochondrial dynamics/function, since Sub2 controls mRNA splicing and Mdm30 regulates mitochondrial aggregation.
Funder
HHS | National Institutes of Health
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
Cited by
8 articles.
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