Chaperone code: Difference between revisions

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== Methylation ==
Chaperone proteins are also regulated by methylation. This can occur through a conformational change (or a change in the structure of the protein), such that the interactions and activity of the protein are changed. <ref name=":1" /><ref>{{Cite journal|last1=Donlin|first1=Laura T.|last2=Andresen|first2=Christian|last3=Just|first3=Steffen|last4=Rudensky|first4=Eugene|last5=Pappas|first5=Christopher T.|last6=Kruger|first6=Martina|last7=Jacobs|first7=Erica Y.|last8=Unger|first8=Andreas|last9=Zieseniss|first9=Anke|last10=Dobenecker|first10=Marc-Werner|last11=Voelkel|first11=Tobias|date=2012-01-15|title=Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization|journal=Genes & Development|volume=26|issue=2|pages=114–119|doi=10.1101/gad.177758.111|issn=0890-9369|pmc=3273835|pmid=22241783}}</ref> For instance, the monomethylation of HSP90 lysine 616 by [[SMPD2|Smyd2]], and its reversal by [[KDM1A|LSD1]], regulate enzymatic activity of HSP90.<ref>{{Cite journal|last1=Abu-Farha|first1=Mohamed|last2=Lanouette|first2=Sylvain|last3=Elisma|first3=Fred|last4=Tremblay|first4=Véronique|last5=Butson|first5=Jeffery|last6=Figeys|first6=Daniel|last7=Couture|first7=Jean-François|date=October 2011|title=Proteomic analyses of the SMYD family interactomes identify HSP90 as a novel target for SMYD2|journal=Journal of Molecular Cell Biology|volume=3|issue=5|pages=301–308|doi=10.1093/jmcb/mjr025|issn=1759-4685|pmid=22028380|doi-access=free}}</ref><ref>{{Cite journal|last1=Rehn|first1=Alexandra|last2=Lawatscheck|first2=Jannis|last3=Jokisch|first3=Marie-Lena|last4=Mader|first4=Sophie L.|last5=Luo|first5=Qi|last6=Tippel|first6=Franziska|last7=Blank|first7=Birgit|last8=Richter|first8=Klaus|last9=Lang|first9=Kathrin|last10=Kaila|first10=Ville R. I.|last11=Buchner|first11=Johannes|date=May 2020|title=A methylated lysine is a switch point for conformational communication in the chaperone Hsp90|journal=Nature Communications|volume=11|issue=1|pages=1219|doi=10.1038/s41467-020-15048-8|issn=2041-1723|pmc=7057950|pmid=32139682|bibcode=2020NatCo..11.1219R}}</ref>
 
==References==