title: The E3 ligase CHIP: insights into its structure and regulation.
abstract: The carboxy-terminus of Hsc70 interacting protein (CHIP) is a cochaperone E3 ligase containing three tandem repeats of tetratricopeptide (TPR) motifs and a C-terminal U-box domain separated by a charged coiled-coil region. CHIP is known to function as a central quality control E3 ligase and regulates several proteins involved in a myriad of physiological and pathological processes. Recent studies have highlighted varied regulatory mechanisms operating on the activity of CHIP which is crucial for cellular homeostasis. In this review article, we give a concise account of our current knowledge on the biochemistry and regulation of CHIP.
authors.affiliation: Cancer Biology and Inflammatory Disorder Division, Council of Scientific and Industrial Research-Indian Institute of Chemical Biology (CSIR-IICB), 4 Raja S.C. Mullick Road, Kolkata 700032, India.
authors.forename: Indranil
authors.initials: I
authors.lastname: Paul
authors.affiliation: Cancer Biology and Inflammatory Disorder Division, Council of Scientific and Industrial Research-Indian Institute of Chemical Biology (CSIR-IICB), 4 Raja S.C. Mullick Road, Kolkata 700032, India.
authors.forename: Mrinal K
authors.initials: MK
authors.lastname: Ghosh
mesh_terms: D000818:Animals; D005786:Gene Expression Regulation; D050883:HSC70 Heat-Shock Proteins / Q000737:chemistry*; D006801:Humans; D007249:Inflammation; D051379:Mice; D018832:Molecular Chaperones / Q000737:chemistry; D010766:Phosphorylation; D011485:Protein Binding; D025941:Protein Interaction Mapping; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000737:chemistry; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry*
chemical_list: D050883:HSC70 Heat-Shock Proteins; D018832:Molecular Chaperones; D025801:Ubiquitin; C467728:STUB1 protein, human; C492951:Stub1 protein, mouse; D044767:Ubiquitin-Protein Ligases