Mild heat and proteotoxic stress promote unique subcellular trafficking and nucleolar accumulation of RGS6 and other RGS proteins. Role of the RGS domain in stress-induced trafficking of RGS proteins. (Q34199055)

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English	Mild heat and proteotoxic stress promote unique subcellular trafficking and nucleolar accumulation of RGS6 and other RGS proteins. Role of the RGS domain in stress-induced trafficking of RGS proteins.	scientific article

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3 November 2019

Mild heat and proteotoxic stress promote unique subcellular trafficking and nucleolar accumulation of RGS6 and other RGS proteins. Role of the RGS domain in stress-induced trafficking of RGS proteins (English)

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Tapan K Chatterjee

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21 May 2003

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3 November 2019

Journal of Biological Chemistry

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30272-30282

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3 November 2019

Evolution of the regulators of G-protein signaling multigene family in mouse and human

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GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins

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The regulator of G protein signaling family

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Slowed recovery of rod photoresponse in mice lacking the GTPase accelerating protein RGS9-1.

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Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs

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RGS-PX1, a GAP for GalphaS and sorting nexin in vesicular trafficking

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Oxidative stress and heat shock stimulate RGS2 expression in 1321N1 astrocytoma cells.

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Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) is required for lipopolysaccharide stimulation of tumor necrosis factor alpha (TNF-alpha) translation: glucocorticoids inhibit TNF-alpha translation by blocking JNK/SAPK.

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RGS12TS-S localizes at nuclear matrix-associated subnuclear structures and represses transcription: structural requirements for subnuclear targeting and transcriptional repression.

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Rapid and reversible relocalization of heat shock factor 1 within seconds to nuclear stress granules

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Novel alternative splicing and nuclear localization of human RGS12 gene products

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Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators

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Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance

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Stress-specific activation and repression of heat shock factors 1 and 2.

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Signal transduction by the JNK group of MAP kinases

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A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C.

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Functional interaction of an axin homolog, conductin, with beta-catenin, APC, and GSK3beta

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Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin

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Erk1/2-dependent phosphorylation of Galpha-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cells

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Roles of the heat shock transcription factors in regulation of the heat shock response and beyond

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Proteasome inhibitor induces nucleolar translocation of Epstein-Barr virus-encoded EBNA-5.

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Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protection

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Directed proteomic analysis of the human nucleolus

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1 reference

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10.1074/JBC.M212688200

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Europe PubMed Central

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3 November 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12761220%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

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