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Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP.

Kundrat L, Regan L.

J Mol Biol. 2010 Jan 22;395(3):587-94. doi: 10.1016/j.jmb.2009.11.017. Epub 2009 Nov 12.


CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates.

Stankiewicz M, Nikolay R, Rybin V, Mayer MP.

FEBS J. 2010 Aug;277(16):3353-67. doi: 10.1111/j.1742-4658.2010.07737.x. Epub 2010 Jul 8.


Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP.

Kundrat L, Regan L.

Biochemistry. 2010 Sep 7;49(35):7428-38. doi: 10.1021/bi100386w.


Ca2+/S100 proteins act as upstream regulators of the chaperone-associated ubiquitin ligase CHIP (C terminus of Hsc70-interacting protein).

Shimamoto S, Kubota Y, Yamaguchi F, Tokumitsu H, Kobayashi R.

J Biol Chem. 2013 Mar 8;288(10):7158-68. doi: 10.1074/jbc.M112.436758. Epub 2013 Jan 23.


Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1.

Shang Y, Xu X, Duan X, Guo J, Wang Y, Ren F, He D, Chang Z.

Biochem Biophys Res Commun. 2014 Mar 28;446(1):387-92. doi: 10.1016/j.bbrc.2014.02.124. Epub 2014 Mar 5.


Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.

Carrello A, Allan RK, Morgan SL, Owen BA, Mok D, Ward BK, Minchin RF, Toft DO, Ratajczak T.

Cell Stress Chaperones. 2004 Summer;9(2):167-81.


Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.

Assimon VA, Southworth DR, Gestwicki JE.

Biochemistry. 2015 Dec 8;54(48):7120-31. doi: 10.1021/acs.biochem.5b00801. Epub 2015 Nov 25.


Biochemical and Proteomic Analysis of Ubiquitination of Hsc70 and Hsp70 by the E3 Ligase CHIP.

Soss SE, Rose KL, Hill S, Jouan S, Chazin WJ.

PLoS One. 2015 May 26;10(5):e0128240. doi: 10.1371/journal.pone.0128240. eCollection 2015 May 26.


Structure and interactions of the helical and U-box domains of CHIP, the C terminus of HSP70 interacting protein.

Xu Z, Devlin KI, Ford MG, Nix JC, Qin J, Misra S.

Biochemistry. 2006 Apr 18;45(15):4749-59.


The chaperone-assisted E3 ligase C terminus of Hsc70-interacting protein (CHIP) targets PTEN for proteasomal degradation.

Ahmed SF, Deb S, Paul I, Chatterjee A, Mandal T, Chatterjee U, Ghosh MK.

J Biol Chem. 2012 May 4;287(19):15996-6006. doi: 10.1074/jbc.M111.321083. Epub 2012 Mar 15.


Hsp70 and Hsp90 multichaperone complexes sequentially regulate thiazide-sensitive cotransporter endoplasmic reticulum-associated degradation and biogenesis.

Donnelly BF, Needham PG, Snyder AC, Roy A, Khadem S, Brodsky JL, Subramanya AR.

J Biol Chem. 2013 May 3;288(18):13124-35. doi: 10.1074/jbc.M113.455394. Epub 2013 Mar 12.


Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes.

Graf C, Stankiewicz M, Nikolay R, Mayer MP.

Biochemistry. 2010 Mar 16;49(10):2121-9. doi: 10.1021/bi901829f.


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

Connell P, Ballinger CA, Jiang J, Wu Y, Thompson LJ, Höhfeld J, Patterson C.

Nat Cell Biol. 2001 Jan;3(1):93-6.


Modulation of heme/substrate binding cleft of neuronal nitric-oxide synthase (nNOS) regulates binding of Hsp90 and Hsp70 proteins and nNOS ubiquitination.

Peng HM, Morishima Y, Pratt WB, Osawa Y.

J Biol Chem. 2012 Jan 6;287(2):1556-65. doi: 10.1074/jbc.M111.323295. Epub 2011 Nov 28.


Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage.

Pratt WB, Morishima Y, Peng HM, Osawa Y.

Exp Biol Med (Maywood). 2010 Mar;235(3):278-89. doi: 10.1258/ebm.2009.009250. Review.


The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.

Alberti S, Böhse K, Arndt V, Schmitz A, Höhfeld J.

Mol Biol Cell. 2004 Sep;15(9):4003-10. Epub 2004 Jun 23.


CHIP functions an E3 ubiquitin ligase of Runx1.

Shang Y, Zhao X, Xu X, Xin H, Li X, Zhai Y, He D, Jia B, Chen W, Chang Z.

Biochem Biophys Res Commun. 2009 Aug 14;386(1):242-6. doi: 10.1016/j.bbrc.2009.06.043. Epub 2009 Jun 12.


Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells.

Kampinga HH, Kanon B, Salomons FA, Kabakov AE, Patterson C.

Mol Cell Biol. 2003 Jul;23(14):4948-58.

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