The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

By P. Connell, C. Ballinger, Jihong Jiang, Yaxu Wu, L. Thompson, J. Höhfeld, C. Patterson. Nature Cell Biology, 2000

1,027 citations recorded by the source corpus.

Subfields: Immunology, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/504717bd7660ab3f365768a1630810328933a948

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

In Materials Chemistry

In Molecular Biology

Citations in the corpus

`The stress of dying': the role of heat shock proteins in the regulation of apoptosis (2004, background): “Previous studies have demonstrated a functional link between the ATP-dependent chaperones Hsp70 and Hsp90 and proteasome-mediated protein degradation via the cooperative activities of the ubiquitin-like co-factor BAG1 and the E3 ligase C-terminal Hsp-interacting protein (CHIP) (Ballinger et al., 199”
HSP90 at the hub of protein homeostasis: emerging mechanistic insights (2010, background): “Much research has focused on one such E3 ubiquitin ligase, C terminus of HSP70-interacting protein ( CHIP ; also known as STUB1), which can ubiquitylate unfolded protein”
Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery 1 (2003, methodology): “presence of CHIP does not achieve the steroid-binding state (160), but that likely reflects CHIP inhibition of hsp70 interaction with the GR before hsp90 can act in the heterocomplex assembly pathway.”
HECT and RING finger families of E3 ubiquitin ligases at a glance (2012, background): “CHIP contains N-terminal tetratricopeptide repeat (TPR) domains that mediate binding to HSP70, HSC70 and HSP90 chaperones (Ballinger et al., 1999; Connell et al., 2001; Nikolay et al., 2004).”
Hsp90: a specialized but essential protein-folding tool. (2001, background): “The existence of CHIP also suggests that like protein folding, protein targeting to the degradation machinery is regulated by additional factors whose functions are not anticipated by a simple kinetic-partitioning model.”
ERAD: the long road to destruction (2005, background): “For instance, CHIP, a soluble U-box ubiquitin ligase, has been implicated in the destruction of ΔF508CFT”
The Hsp70 chaperone machinery: J-proteins as drivers of functional specificity (2010, neutral): “However, hs CHIP's biochemical properties and the results of in vivo experiments suggest a more specific role in the targeted degradation of HSP90 client”