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Study reports that STUB1 regulates gastric cancers (GC) cell proliferation and response to therapeutic drugs through YAP1. STUB1 is responsible for YAP1 ubiquitination at K280 and degradation. Downregulation of STUB1 promoted GC proliferation, tumorigenesis, and chemoresistance in a YAP1-dependent manner. STUB1 expression inversely correlates with YAP1 in GC, suggesting a role for the STUB1-YAP1 axis in GC pathogenesis.
Phosphatase PGAM5 (phosphoglycerate mutase 5) and deubiquitinase OTUB1 (ovarian tumor domain containing ubiquitin aldehyde binding protein 1) were confirmed as E4B substrates, and beta-catenin and CDK4 (cyclin-dependent kinase 4) were confirmed as CHIP substrates.
We report a heterozygous STUB1 pathogenic genetic variant causing dominant cerebellar ataxia
IRS4, as a new substrate of CHIP, is negatively regulated by CK1gamma2 at the posttranslational level.
The existence of a multiprotein complex containing UBXN2A, CHIP, and mot-2 suggests a synergistic tumor suppressor activity of UBXN2A and CHIP in mot-2-enriched tumors.
CHIP depletion inhibited cell growth, migration and invasion potential of colorectal cancer cells, accompanied by downregulation of MAPK and AKT signaling activities and upregulation of E-cadherin.
CHIP negatively regulates cathepsin B protein/cathepsin L protein expression in ErbB2(+) and other breast cancer cell lines. cathepsin B protein inhibition abrogates invasion and matrix degradation in vitro and halts ErbB2(+) breast cancer cell line xenograft growth.
the present study demonstrates that covalent ISG15 conjugation produces a novel CHIP regulatory mode that enhances the tumor-suppressive activity of CHIP.
Our results provide the first evidence for a mediator function of cIAP1 and collaborative activity of cIAP1 and CHIP, suggesting that maintaining balanced levels of these E3 ligases might be beneficial for normal cell growth.
K6-linked ubiquitylation of FADD by CHIP is a crucial checkpoint in cytokine-dependent extrinsic apoptosis.
ORP150 and CHIP demonstrate antagonism under normal and stress conditions wherein they inversely regulate each other thus affecting BACE1 level.
Data suggest that the molecular basis of genetic defects in CHIP that cause SCAR16 is that most mutations observed in patients with SCAR16 result in destabilization of CHIP leading to down-regulation of it's biquitination function. (SCAR16 = spinocerebellar ataxia autosomal recessive type 16)
these findings suggest that CHIP plays a role in negative regulation of PINK1 stability and may suppress PINK1's cytoprotective effect during staurosporine-induced mammalian cell death.
Results identified a new role of CHIP in adipocyte differentiation. CHIP interacts with and mediates the ubiquitylation of PPARgamma , which results in negative effects on adipogenesis.
The overexpression of CHIP significantly increased the migration and invasion of the DU145 cells, which is possible due to activation of the AKT signaling pathway and upregulation of vimentin. The expression level of CHIP was observed to be increased in human prostate cancer tissues compared with the adjacent normal tissue.
Here the authors show that the mammalian ubiquitin ligase C-terminal Hsp70-interacting protein (CHIP), if freed from chaperones during acute stress, can dock on cellular membranes thus performing a proteostasis sensor function.
These results suggest that in the early response to stressful stimuli, MLK4beta-MLK3 binding is important for regulating MLK3 activity and MAPK signalling, and after prolonged periods of stress exposure, MLK4beta and MLK3 proteins decline via CHIP-dependent degradation.
Prostate cancer cells expressing an S273A mutant of CHIP have attenuated AR degradation upon 2-ME treatment compared with cells expressing wild-type CHIP, supporting the idea that CHIP phosphorylation by Aurora A activates its E3 ligase activity for the AR
CHIP role in lung cancer radioresistance.p21 is a bona fide ubiquitylation substrate for CHIP.
PC-1 works in conjunction with E3 ligase CHIP to regulate androgen receptor stability and activity.
Proteomic analysis of WT and CHIP KO mouse brains reveals proteins essential for maintaining energetic, redox, and mitochondrial homeostasis undergo genotype-dependent expression changes. CHIP is an essential regulator of mitochondrial number,signaling, survival.
In summary, these results suggest that CHIP regulates AQP2 and subsequently, renal water handling.
Study using two rodent models demonstrated that T246M mutation (described in autosomal recessive spinocerebellar ataxia-16 patients) results in structural disorganization and misfolding of the CHIP U-box domain, promoting oligomerization, and increased proteasome-dependent turnover. CHIP-T246M has no ligase activity but maintains interactions with chaperones and chaperone-related functions.
MLL5 has a role in suppressing antiviral innate immune response by facilitating STUB1-mediated RIG-I degradation
these results indicate that phosphorylation of CHIP at Ser20 by Cdk5 activation inhibits CHIP-mediated truncated apoptosis-inducing factor (tAIF) degradation, thereby contributing to tAIF-induced neuronal cell death following rotenone treatment
CHIP was as a master regulator of AQP2 degradation via HSP70 that has dual functions: (1) as chaperone for AQP2 and (2) as an anchoring protein for MDM2 E3 ligase, which is likely to be involved in AQP2 degradation.
Consistent with reduced transcription factor EB (TFEB) activity, accumulation of phosphorylated TFEB in STUB1-deficient cells resulted in reduced autophagy and reduced mitochondrial biogenesis. These studies reveal that the ubiquitin-proteasome pathway participates in regulating autophagy and lysosomal functions by regulating the activity of TFEB.
ACR 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, and CRL4(CRBN), which is formed by Cul4a/b, Ddb1, and Crbn, and interacts with the COOH terminus of the ACR via Crbn.
The chaperone protein Hsp70 was found to be important for CHIP and NUCB1 interaction as well as CHIP-mediated NUCB1 down-regulation.
CHIP is a negative regulator of RIPK1 and RIPK3, thus inhibiting necroptosis.
our study demonstrated that over-expressing miR-21 in UCBMSCs could improve neovascularization in Critical limb ischemia (CLI) through enhancing HIF-1alpha activity by targeting CHIP, which may hold great therapeutic promise in treating CLI
PABPN1 interacts with and is stabilized by heat shock protein 90.
CHIP is an essential regulator of neuronal bioenergetics and redox tone.
CHIP targets Osx for ubiquitination and degradation in osteoblasts after chronic exposure to TNF-alpha.
CHIP/TRAF3/NIK interactions recruit NIK to E3 ligase complexes for ubiquitination and degradation, thus maintaining NIK at low levels
Cbl-b, together with Stub1, ubiquitinate Foxp3, and regulate tTreg development.
CHIP regulates the levels of FMR1 as an E3 ubiquitin ligase in phosphorylation-dependent manner, suggesting that CHIP regulates FMR1-mediated translational repression by regulating the levels of FMR1.
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
CLL-associated antigen KW-8
, E3 ubiquitin-protein ligase CHIP
, STIP1 homology and U box-containing protein 1
, antigen NY-CO-7
, carboxy terminus of Hsp70-interacting protein
, heat shock protein A binding protein 2 (c-terminal)
, serologically defined colon cancer antigen 7
, STIP1 homology and U-Box containing protein 1
, STIP1 homology and U-box containing protein 1