Chaperone code: Difference between revisions

Revision as of 02:50, 19 August 2020

Revision as of 02:59, 19 August 2020

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== Phosphorylation ==

Phosphorylation of chaperone proteins can affect their activity. [[Hsp70|HSP70]], a major chaperone protein, was identified in 2012 as a hotspot of phospho-regulation. <ref>{{Cite journal|last=Beltrao|first=Pedro|last2=Albanèse|first2=Véronique|last3=Kenner|first3=Lillian R.|last4=Swaney|first4=Danielle L.|last5=Burlingame|first5=Alma|last6=Villén|first6=Judit|last7=Lim|first7=Wendell A.|last8=Fraser|first8=James S.|last9=Frydman|first9=Judith|last10=Krogan|first10=Nevan J.|date=2012-07-20|title=Systematic Functional Prioritization of Protein Posttranslational Modifications|url=https://www.cell.com/cell/abstract/S0092-8674(12)00706-4|journal=Cell|language=English|volume=150|issue=2|pages=413–425|doi=10.1016/j.cell.2012.05.036|issn=0092-8674|pmid=22817900}}</ref> Subsequently, phosphorylation of chaperone protein [[Hsp70|HSP70]] by a cyclin dependent kinase was shown to be delay [[cell cycle]] progression in yeast and mammals by altering [[Cyclin D1]] stability (a key regulator of the cell cycle). <ref>{{Cite journal|last=Truman|first=Andrew W.|last2=Kristjansdottir|first2=Kolbrun|last3=Wolfgeher|first3=Donald|last4=Hasin|first4=Naushaba|last5=Polier|first5=Sigrun|last6=Zhang|first6=Hong|last7=Perrett|first7=Sarah|last8=Prodromou|first8=Chrisostomos|last9=Jones|first9=Gary W.|last10=Kron|first10=Stephen J.|date=2012-12-07|title=CDK-Dependent Hsp70 Phosphorylation Controls G1 Cyclin Abundance and Cell-Cycle Progression|url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3778871/|journal=Cell|volume=151|issue=6|pages=1308–1318|doi=10.1016/j.cell.2012.10.051|issn=0092-8674|pmc=3778871|pmid=23217712}}</ref>