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The '''chaperone code''' refers to [[Post-translational modification|post-translational modifications]] of molecular [[Chaperone (protein)|chaperones]] that control protein folding. Whilst the [[genetic code]] specifies how [[DNA]] makes proteins, and the [[histone code]] regulates histone-DNA interactions, the chaperone code controls how proteins are folded to produce a functional [[proteome]].<ref name=":0">{{Cite journal|last1=Nitika|last2=Porter|first2=Corey M.|last3=Truman|first3=Andrew W.|last4=Truttmann|first4=Matthias C.|date=2020-07-31|title=Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code|journal=The Journal of Biological Chemistry|volume=295|issue=31|pages=10689–10708|doi=10.1074/jbc.REV120.011666|issn=0021-9258|pmc=7397107|pmid=32518165|doi-access=free }}</ref><ref name=":1">{{Cite journal|last1=Backe|first1=Sarah J.|last2=Sager|first2=Rebecca A.|last3=Woodford|first3=Mark R.|last4=Makedon|first4=Alan M.|last5=Mollapour|first5=Mehdi|date=2020-08-07|title=Post-translational modifications of Hsp90 and translating the chaperone code|journal=The Journal of Biological Chemistry|volume=295|issue=32|pages=11099–11117|doi=10.1074/jbc.REV120.011833|issn=0021-9258|pmc=7415980|pmid=32527727|doi-access=free }}</ref>
The chaperone code refers to the combinatorial array of [[Post-translational modification|post-translational modifications]] (enzymes add chemical modifications to amino acids that change their properties) —i.e. [[phosphorylation]], [[acetylation]], [[Ubiquitin|ubiquitination]], [[methylation]], etc.—that are added to molecular chaperones to modulate their activity. Molecular chaperones are proteins specialized in folding and unfolding of the other cellular proteins, and the assembly and dismantling of protein complexes. This is critical in the regulation of protein-protein interactions and many cellular functions. Because post-translational modifications are marks that can be added and removed rapidly, they provide an efficient mechanism to explain the plasticity observed in proteome organization during cell growth and development.
The chaperone code concept posits that combinations of post-translational modifications at the surface of chaperones, including phosphorylation, acetylation,<ref name=":0" />
1) [[Substrate (chemistry)|chaperone-substrate]] affinity and specificity
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3) chaperone localization
4) chaperone-co-chaperone interaction
== Levels of the Chaperone Code ==
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== Phosphorylation ==
Site-specific [[Protein phosphorylation|phosphorylation]] of chaperone proteins can affect their activity. In some cases phosphorylation may disrupt the interaction with a co-chaperone protein thus negatively affecting its activity. In other instances it may promote the activation of particular chaperone targets (referred to as clients).<ref>{{Cite journal|last1=Woodford|first1=Mark R.|last2=Truman|first2=Andrew W.|last3=Dunn|first3=Diana M.|last4=Jensen|first4=Sandra M.|last5=Cotran|first5=Richard|last6=Bullard|first6=Renee|last7=Abouelleil|first7=Mourad|last8=Beebe|first8=Kristin|last9=Wolfgeher|first9=Donald|last10=Wierzbicki|first10=Sara|last11=Post|first11=Dawn E.|date=2016-02-02|title=Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors|journal=Cell Reports|volume=14|issue=4|pages=872–884|doi=10.1016/j.celrep.2015.12.084|issn=2211-1247|pmc=4887101|pmid=26804907}}</ref> Enzymes such as [[protein kinase A]], casein kinase 1 and 2 ([[Casein kinase 1|CK1]] and [[Casein kinase 2|CK2]]), and [[GSK3B|glycogen synthase kinase B]] serve as kinases for chaperone proteins.<ref name=":1" /> [[Hsp70|HSP70]], a major chaperone protein, was identified in 2012 as a hotspot of phospho-regulation.<ref>{{Cite journal|last1=Beltrao|first1=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=
== Methylation ==
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