STUB1 (STIP1 homology and U-Box containing protein 1) is a human gene that codes for the protein CHIP (C terminus of HSC70-Interacting Protein).[5][6]
Function
The CHIP protein encoded by this gene binds to and inhibits the
ATPase activity of the
chaperone proteinsHSC70 and
HSP70 and blocks the forward reaction of the HSC70-HSP70 substrate-binding cycle.[6] In addition, CHIP possesses
E3 ubiquitin ligase activity and promotes
ubiquitylation,[7] mainly of chaperone-bound misfolded proteins.
CHIP enhances HSP70 induction during acute stress and also mediates its turnover during the stress recovery process. Hence CHIP appears to maintain protein homeostasis by controlling chaperone levels during stress and recovery.[8]
Mutations in STUB1 cause spinocerebellar
ataxiatype 16.[9]
Cardozo CP, Michaud C, Ost MC, Fliss AE, Yang E, Patterson C, Hall SJ, Caplan AJ (Feb 2003). "C-terminal Hsp-interacting protein slows androgen receptor synthesis and reduces its rate of degradation". Archives of Biochemistry and Biophysics. 410 (1): 134–40.
doi:
10.1016/S0003-9861(02)00680-X.
PMID12559985.
Galigniana MD, Harrell JM, Housley PR, Patterson C, Fisher SK, Pratt WB (Apr 2004). "Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation". Brain Research. Molecular Brain Research. 123 (1–2): 27–36.
doi:
10.1016/j.molbrainres.2003.12.015.
hdl:11336/29101.
PMID15046863.
STUB1 (STIP1 homology and U-Box containing protein 1) is a human gene that codes for the protein CHIP (C terminus of HSC70-Interacting Protein).[5][6]
Function
The CHIP protein encoded by this gene binds to and inhibits the
ATPase activity of the
chaperone proteinsHSC70 and
HSP70 and blocks the forward reaction of the HSC70-HSP70 substrate-binding cycle.[6] In addition, CHIP possesses
E3 ubiquitin ligase activity and promotes
ubiquitylation,[7] mainly of chaperone-bound misfolded proteins.
CHIP enhances HSP70 induction during acute stress and also mediates its turnover during the stress recovery process. Hence CHIP appears to maintain protein homeostasis by controlling chaperone levels during stress and recovery.[8]
Mutations in STUB1 cause spinocerebellar
ataxiatype 16.[9]
Cardozo CP, Michaud C, Ost MC, Fliss AE, Yang E, Patterson C, Hall SJ, Caplan AJ (Feb 2003). "C-terminal Hsp-interacting protein slows androgen receptor synthesis and reduces its rate of degradation". Archives of Biochemistry and Biophysics. 410 (1): 134–40.
doi:
10.1016/S0003-9861(02)00680-X.
PMID12559985.
Galigniana MD, Harrell JM, Housley PR, Patterson C, Fisher SK, Pratt WB (Apr 2004). "Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation". Brain Research. Molecular Brain Research. 123 (1–2): 27–36.
doi:
10.1016/j.molbrainres.2003.12.015.
hdl:11336/29101.
PMID15046863.