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Papers In Press, published online ahead of print May 21, 2003
Department of Pharmacology, University of Iowa College of Medicine, Iowa City, IA 52242
Corresponding Author: rory-fisher{at}uiowa.edu
RGS proteins negatively regulate heterotrimeric G protein signaling. The hallmark structural domain of this protein family, the RGS domain, confers GAP activity toward heterotrimeric G protein. RGS6 is a member of the R7 subfamily of RGS proteins possessing DEP (Drosophilla/EGL10/Pleckstrin) homology and GGL (G protein g subunit-like) domains in addition to the RGS domain. Our previous study documented unusual complexity in splicing of the human RGS6 gene. Here we provide new evidence that mild heat- or proteotoxic stress induces relocalization of RGS6 proteins to nucleoli. This response was observed in COS-7 cells expressing various splice forms of RGS6, was observed in cells treated with p38 kinase inhibitor SB203580 or co-expressing a dominant negative kinase inactive SAPK. The RGS domain of RGS6 was identified as one structural module providing support for its stress-induced nucleolar trafficking, and various other RGS proteins or their isolated RGS domains similarly undergo nucleolar migration in response to heat- or proteotoxic stress. The atypical RGS domains of axin and AKAP10 also underwent stress-induced nucleolar trafficking while structural domains outside of the RGS domain of some RGS proteins can override nucleolar trafficking in response to stress. Inhibition of rDNA transcription also promoted nucleolar migration of RGS6, a response observed in a subset of nucleolar proteins. The DEP domain of RGS6, present in R7 RGS members, but not its RGS domain, conferred structural support for its transcription-linked nucleolar migration. RGS6 exhibited trafficking from subnuclear dots to nucleoli in response to heat-, proteotoxic- or transcription-linked stress. RGS6 fused to a Gal4 DNA binding domain markedly repressed reporter gene expression from a Gal4-E1b-TATA promoter. These results provide new evidence that mammalian RGS and other RGS proteins undergo unique subcellular trafficking in response to specific forms of cellular stress and implicate the RGS family of proteins in cellular stress signaling pathways.
J. Biol. Chem, 10.1074/jbc.M212688200
Submitted on December 12, 2002
Revised on May 16, 2003
Accepted on May 21, 2003
Mild heat - and proteotoxic stress promote unique subcellular trafficking and nucleolar accumularion of RGS6 and other RGS proteins: Role of the RGS domain in stress-induced trafficking of RGS proteins
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