Hsp70-binding protein 1

Definition:

Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.

References:

[1]. D A Raynes, et al. Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):203-7. [Content Brief]

[2]. D A Raynes, et al. Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein. J Biol Chem. 1998 Dec 4;273(49):32883-8. [Content Brief]

[3]. Denis V Yashin, et al. The heat shock-binding protein (HspBP1) protects cells against the cytotoxic action of the Tag7-Hsp70 complex. J Biol Chem. 2011 Mar 25;286(12):10258-64. [Content Brief]

[4]. Catherine A McLellan, et al. HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain. J Biol Chem. 2003 May 23;278(21):19017-22. [Content Brief]

[5]. Simon Alberti, et al. The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Mol Biol Cell. 2004 Sep;15(9):4003-10. [Content Brief]

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