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B83 - Investigation of neurodegenerative diseases via the CHIP:HSP70 complex
Heat Shock Protein 70 (Hsp70) is a chaperone protein that works to maintain cellular homeostasis through folding and refolding proteins.
B83 - Investigation of neurodegenerative diseases via the CHIP:HSP70 complex
Mentor(s): Richard Page, Ph.D.
Heat Shock Protein 70 (Hsp70) is a chaperone protein that works to maintain cellular homeostasis through folding and refolding proteins. These proteins are vital in the cell’s response to stress via their ability to refold misfolded proteins. Hsp70 also has a key role in the protein degradation pathway, working with cochaperone proteins, such as CHIP, to ubiquitinate proteins to send them to be degraded. CHIP and Hsp70 bind together, forming the CHIP:Hsp70 capable of performing these tasks. CHIP autoubiquitinates itself when it is no longer needed. This autoubiquitination leads to its own degradation. CHIP has 9 known Lysine residues capable of ubiquitination. This ubiquitination leads to the dissociation of the CHIP/Hsp70 complex.