Molecular chaperones: Guardians of tumor suppressor stability and function (IMAGE)
Caption
Figure 1: The molecular chaperone network. Client proteins rely on sequential interactions with chaperones, cochaperones, and chaperonins to fold into an active, native, state. Thus, functional levels of client proteins are tightly regulated by this process. The chaperones, cochaperones, and chaperonins commonly involved in the chaperoning of tumor suppressor proteins are shown; however, the exact number and types of molecular chaperone network members necessary for proper chaperoning is client-specific. Abbreviations: Hsp70: heat-shock protein 70; HOP: Hsp70-Hsp90 organizing protein; TRiC: tailless complex polypeptide 1 ring complex; Hsp90: heat-shock protein 90; Aha1: Activator of Hsp90 ATPase.
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2024 Heritz et al.
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