Protein arginylation regulates cellular stress response by stabilizing HSP70 and HSP40 transcripts
نویسندگان
چکیده
منابع مشابه
Mesothelioma Cells Escape Heat Stress by Upregulating Hsp40/Hsp70 Expression via Mitogen-Activated Protein Kinases
Therapy with hyperthermal chemotherapy in pleural diffuse malignant mesothelioma had limited benefits for patients. Here we investigated the effect of heat stress on heat shock proteins (HSP), which rescue tumour cells from apoptosis. In human mesothelioma and mesothelial cells heat stress (39-42 degrees C) induced the phosphorylation of two mitogen activated kinases (MAPK) Erk1/2 and p38, and ...
متن کاملProtein modification by arginylation.
The modification of protein by arginine catalyzed by arginyltransferases (ATE1) described by the Kashina group in this issue shows that arginylation of protein occurs widely in biology and is being recognized as a key regulatory reaction such as phosphorylation of proteins (Wang et al., 2011).
متن کاملArginylation: a new regulator of mRNA stability and heat stress response
Cellular stress responses are protective mechanism against diverse environmental and physiological factors, which cause macromolecular damage in cells. Different stress conditions, including heat stress, oxidative stress, and ER stress, are associated with denatured or unfolded proteins, which are recognized by molecular chaperons like heat shock proteins (HSPs). Interaction of unfolded protein...
متن کاملBinding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in protein homeostasis. In these various tasks, the activity of Hsp70 is shaped by interactions with co-chaperones, such as Hsp40. The Hsp40 family of co-chaperones binds to Hsp70 through a conserved J-domain, and these factors stimulate ATPase and protein-folding activity. Using chemical screens, ...
متن کاملHsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.
Self-templating amyloid forms of Sup35 constitute the yeast prion [PSI(+)]. How the protein-remodelling factor, Hsp104, collaborates with other chaperones to regulate [PSI(+)] inheritance remains poorly delineated. Here, we report how the Ssa and Ssb components of the Hsp70 chaperone system directly affect Sup35 prionogenesis and cooperate with Hsp104. We identify the ribosome-associated Ssb1:Z...
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ژورنال
عنوان ژورنال: Cell Death Discovery
سال: 2016
ISSN: 2058-7716
DOI: 10.1038/cddiscovery.2016.74