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E3 ubiquitin-protein ligase CHIP

Definition:

E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome. Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation. May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation. Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation.

References:

[1]. Jason L Parsons, et al. Ubiquitin ligase ARF-BP1/Mule modulates base excision repair. EMBO J. 2009 Oct 21;28(20):3207-15. [Content Brief]

[2]. Riccardo Mezzadra, et al. Identification of CMTM6 and CMTM4 as PD-L1 protein regulators. Nature. 2017 Sep 7;549(7670):106-110. [Content Brief]

[3]. Ji Hae Seo, et al. ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation. Nat Commun. 2016 Oct 6;7:12882. [Content Brief]

[4]. P Connell, et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol. 2001 Jan;3(1):93-6. [Content Brief]

[5]. Yu Shang, et al. Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1. Biochem Biophys Res Commun. 2014 Mar 28;446(1):387-92. [Content Brief]

[6]. Hwei-Ming Peng, et al. Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase. J Biol Chem. 2004 Dec 17;279(51):52970-7. [Content Brief]

[7]. Sarah M Ronnebaum, et al. The ubiquitin ligase CHIP prevents SirT6 degradation through noncanonical ubiquitination. Mol Cell Biol. 2013 Nov;33(22):4461-72. [Content Brief]

[8]. Philipp Christoph Janiesch, et al. The ubiquitin-selective chaperone CDC-48/p97 links myosin assembly to human myopathy. Nat Cell Biol. 2007 Apr;9(4):379-90. [Content Brief]

[9]. Seung-Won Choi, et al. PELI1 Selectively Targets Kinase-Active RIP3 for Ubiquitylation-Dependent Proteasomal Degradation. Mol Cell. 2018 Jun 7;70(5):920-935.e7. [Content Brief]

[10]. J Jiang, et al. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J Biol Chem. 2001 Nov 16;276(46):42938-44. [Content Brief]

[11]. Michael K Pabarcus, et al. CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases. Arch Biochem Biophys. 2009 Mar 1;483(1):66-74. [Content Brief]

[12]. Balasubramaniam Annamalai, et al. Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis. Mol Cancer Res. 2009 Jul;7(7):1021-32. [Content Brief]

[13]. Zuojia Chen, et al. The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3. Immunity. 2013 Aug 22;39(2):272-85. [Content Brief]

[14]. Yoshihiro Matsumura, et al. Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase. J Biol Chem. 2013 Oct 25;288(43):31069-79. [Content Brief]

[15]. C A Ballinger, et al. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol. 1999 Jun;19(6):4535-45. [Content Brief]

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