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Through selective degradation of Clp subunits, AtCHIP could positively regulate homeostasis of Clp proteolytic subunits and maximize the production of functional chloroplasts. Similar results were obtained from transgenic tobacco plants.
we propose that CHIP and NBR1 (show NBR1 Proteins) mediate two distinct but complementary anti-proteotoxic pathways and protein's propensity to aggregate under stress conditions is one of the critical factors for pathway selection of protein degradation
Hsc70-4 and CHIP were highly induced in ppi2 mutant plants, where they mediated the degradation of chloroplast-targeted precursors through the ubiquitin-26S proteasome (show Psmd4 Proteins) system.
AtCHIP, an E3 ubiquitin liagase, functions upstream of protein phosphatase 2A in stress-responsive signal transduction pathways under conditions of low temperature or in the dark. [AtCHIP]
The interaction of CHIP with FtsH1 in vitro, in normal and in CHIP-over-expressing plants is reported.
ACR (show ACR Proteins) interacts with proteins that regulate the ubiquitin-proteasome system, predominantly with the E3 ubiquitin-protein ligases Stub1, which binds the NH2 terminus of the ACR (show ACR Proteins), and CRL4(CRBN (show CRBN Proteins)), which is formed by Cul4a (show CUL4A Proteins)/b, Ddb1 (show DDB1 Proteins), and Crbn (show CRBN Proteins), and interacts with the COOH terminus of the ACR (show ACR Proteins) via Crbn (show CRBN Proteins).
The chaperone protein Hsp70 (show HSP70 Proteins) was found to be important for CHIP and NUCB1 (show NUCB1 Proteins) interaction as well as CHIP-mediated NUCB1 (show NUCB1 Proteins) down-regulation.
CHIP is a negative regulator of RIPK1 (show RIPK1 Proteins) and RIPK3 (show RIPK3 Proteins), thus inhibiting necroptosis.
our study demonstrated that over-expressing miR (show MLXIP Proteins)-21 in UCBMSCs could improve neovascularization in Critical limb ischemia (CLI (show CLU Proteins)) through enhancing HIF-1alpha (show HIF1A Proteins) activity by targeting CHIP, which may hold great therapeutic promise in treating CLI (show CLU Proteins)
PABPN1 (show PABPN1 Proteins) interacts with and is stabilized by heat shock protein 90 (show HSP90 Proteins).
CHIP targets Osx (show SP7 Proteins) for ubiquitination and degradation in osteoblasts after chronic exposure to TNF-alpha (show TNF Proteins).
CHIP/TRAF3 (show TRAF3 Proteins)/NIK (show MAP4K4 Proteins) interactions recruit NIK (show MAP4K4 Proteins) to E3 ligase complexes for ubiquitination and degradation, thus maintaining NIK (show MAP4K4 Proteins) at low levels
Cbl-b, together with Stub1, ubiquitinate Foxp3 (show FOXP3 Proteins), and regulate tTreg development.
CHIP regulates the levels of FMR1 (show FMR1 Proteins) as an E3 ubiquitin ligase (show MUL1 Proteins) in phosphorylation-dependent manner, suggesting that CHIP regulates FMR1 (show FMR1 Proteins)-mediated translational repression by regulating the levels of FMR1 (show FMR1 Proteins).
The cardiac CHIP appears to play a role in regulating autophagy during the development of cardiac hypertrophy, possibly by its role in supporting Akt (show AKT1 Proteins) signalling, induced by voluntary running in vivo.
C terminus of Hsc70-interacting protein (show ST13 Proteins) (CHIP) selectively interacted with epidermal growth factor receptor (EGFR (show EGFR Proteins)) mutants and simultaneously induced their ubiquitination and proteasomal degradation.
Study reveals an important function of CHIP-mediated proteolysis in insulin (show INS Proteins) and IGF1 (show IGF1 Proteins) signaling; upon proteotoxic stress conditions and during aging, CHIP is recruited toward disposal of misfolded proteins, reducing its capacity to degrade the INSR (show INSR Proteins); identify a degradation pathway that controls the level of active DAF-2 (show INSR Proteins)/INSR (show INSR Proteins) in C. elegans, Drosophila and human cells.
Overexpression of CHIP decreased intracellular protein (show CKAP2 Proteins) levels of both G2385R mutant and wild-type LRRK2 (show LRRK2 Proteins), while short interfering RNA CHIP knockdown had the opposite effect
CHIP directly regulates the stability of CD166 protein through the ubiquitin proteasome system.
Data show that BAG2 (show BAG2 Proteins) Inhibits CHIP-Mediated HSP72 (show HSPA1A Proteins) ubiquitination in aged cells.
Data show that transcription factor regulatory factor X 1 (RFX1 (show RFX1 Proteins)) protein expression can be tightly regulated by polyubiquitination-mediated proteosomal degradation via STIP1 homology and U-box containing protein 1 (STUB1).
CHIP may serve as a promising prognostic biomarker for non-small cell lung cancer (NSCLC] patients and it may be involved in NSCLC angiogenesis through regulating VEGF (show VEGFA Proteins) secretion and expression of VEGFR2 (show KDR Proteins).
Cdk5 (show CDK5 Proteins)-mediated phosphorylation of CHIP negatively regulates its neuroprotective function, thereby contributing to neuronal cell death progression following neurotoxic stimuli.
CHIP is a bona fide negative regulator of the RIPK1 (show RIPK1 Proteins)-RIPK3 (show RIPK3 Proteins) necrosome formation leading to desensitization of TNF (show TNF Proteins)-mediated necroptosis
Protein-protein interactions modulate the docking-dependent E3-ubiquitin ligase (show MUL1 Proteins) activity of CHIP.
STUB1, or CHIP, is a ubiquitin ligase/cochaperone that participates in protein quality control by targeting a broad range of chaperone protein substrates for degradation (Min et al., 2008
STIP1 homology and U-box containing protein 1
, STIP1 homology and U box-containing protein 1
, E3 ubiquitin-protein ligase CHIP
, carboxy terminus of Hsp70-interacting protein
, CLL-associated antigen KW-8
, antigen NY-CO-7
, heat shock protein A binding protein 2 (c-terminal)
, serologically defined colon cancer antigen 7
, STIP1 homology and U-Box containing protein 1