Understanding chaperone specificity: evidence for a 'client code'

Siddhi Omkar; Ainella Rysbayeva; Andrew W Truman

doi:10.1016/j.tibs.2023.05.008

Understanding chaperone specificity: evidence for a 'client code'

Trends Biochem Sci. 2023 Aug;48(8):662-664. doi: 10.1016/j.tibs.2023.05.008. Epub 2023 Jun 15.

Authors

Siddhi Omkar¹, Ainella Rysbayeva¹, Andrew W Truman²

Affiliations

¹ Department of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC 28223, USA.
² Department of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC 28223, USA. Electronic address: atruman1@uncc.edu.

Abstract

The interactions of molecular chaperones with clients can be regulated by chaperone post-translational modification (PTMs) collectively known as the 'chaperone code'. What is less understood is how PTMs on client proteins may impact chaperone-client interactions. In this forum, we discuss the possibility of a 'client code'.

Keywords: Hsp70; Hsp90; chaperones; client; phosphorylation; post-translational modification.

MeSH terms

HSP70 Heat-Shock Proteins / metabolism
HSP90 Heat-Shock Proteins* / genetics
HSP90 Heat-Shock Proteins* / metabolism
Humans
Molecular Chaperones* / metabolism
Protein Binding
Protein Processing, Post-Translational

Substances

HSP90 Heat-Shock Proteins
Molecular Chaperones
HSP70 Heat-Shock Proteins

Abstract

MeSH terms

Substances

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