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https://www.readbyqxmd.com/read/28536143/aurora-kinase-a-promotes-ar-degradation-via-the-e3-ligase-chip
#1
James M Larner, Sukumar Sarkar, David L Brautigan
Reducing the levels of the androgen receptor (AR) is one of the most viable approaches to combat castration-resistant prostate cancer (CRPC). Previously, we observed that proteasomal-dependent degradation of AR in response to 2-methoxyestradiol (2-ME) depends primarily on the E3 ligase C-terminus of HSP70-interacting protein (STUB1/CHIP). Here, 2-ME stimulation activates CHIP by phosphorylation via Aurora kinase A (AURKA). Aurora A kinase inhibitors and RNAi knockdown of Aurora A transcript selectively blocked CHIP phosphorylation and AR degradation...
May 23, 2017: Molecular Cancer Research: MCR
https://www.readbyqxmd.com/read/28441527/proteostasis-or-aging-let-the-chips-fall-where-they-may
#2
Robyn Branicky, Siegfried Hekimi
The conserved E3 ubiquitin ligase CHIP/CHN-1 contributes to proteostasis by ubiquitylating HSP70 and HSP90-interacting proteins. In a recent issue of Cell,Tawo et al. (2017) show that CHIP/CHN-1 also directly ubiquitylates the insulin receptor INSR/DAF-2 to regulate its turnover. These findings suggest an unexpected interpretation of the effects of altered proteostasis on survival.
April 24, 2017: Developmental Cell
https://www.readbyqxmd.com/read/28337377/the-e3-ubiquitin-ligase-chip-mir-92b-pten-regulatory-network-contributes-to-tumorigenesis-of-glioblastoma
#3
Tao Xu, Hongxiang Wang, Mei Jiang, Yong Yan, Weiqing Li, Hanchong Xu, Qilin Huang, Yicheng Lu, Juxiang Chen
Glioblastoma (GBM) is the most frequent, aggressive and fatal tumor in the central nervous system, while PTEN signaling is frequently deregulated in human GBM. We previously reported the up-regulation of the carboxyl terminal of Hsp70-interacting protein (CHIP) in GBM, however, the causal link between its dysregulation and tumorigenesis has not been established. Using miRNA microarrays and quantitative RT-PCR (qRT-PCR), we found activation of CHIP leads to increased transcription of miR-92b. Further studies in T98G and LN229 cells showed overexpression of miR-92b elicited reduction of PTEN and efficiently rescued glioma development in CHIP knock-down cells...
2017: American Journal of Cancer Research
https://www.readbyqxmd.com/read/28320739/a-covalently-bound-inhibitor-triggers-ezh2-degradation-through-chip-mediated-ubiquitination
#4
Xu Wang, Wei Cao, Jianjun Zhang, Ming Yan, Qin Xu, Xiangbing Wu, Lixin Wan, Zhiyuan Zhang, Chenping Zhang, Xing Qin, Meng Xiao, Dongxia Ye, Yuyang Liu, Zeguang Han, Shaomeng Wang, Li Mao, Wenyi Wei, Wantao Chen
Enhancer of zeste homolog 2 (EZH2) has been characterized as a critical oncogene and a promising drug target in human malignant tumors. The current EZH2 inhibitors strongly suppress the enhanced enzymatic function of mutant EZH2 in some lymphomas. However, the recent identification of a PRC2- and methyltransferase-independent role of EZH2 indicates that a complete suppression of all oncogenic functions of EZH2 is needed. Here, we report a unique EZH2-targeting strategy by identifying a gambogenic acid (GNA) derivative as a novel agent that specifically and covalently bound to Cys668 within the EZH2-SET domain, triggering EZH2 degradation through COOH terminus of Hsp70-interacting protein (CHIP)-mediated ubiquitination...
May 2, 2017: EMBO Journal
https://www.readbyqxmd.com/read/28278223/the-structure-of-fkbp38-in-complex-with-the-meevd-tetratricopeptide-binding-motif-of-hsp90
#5
Katie L I M Blundell, Mohinder Pal, S Mark Roe, Laurence H Pearl, Chrisostomos Prodromou
Tetratricopeptide (TPR) domains are known protein interaction domains. We show that the TPR domain of FKBP8 selectively binds Hsp90, and interactions upstream of the conserved MEEVD motif are critical for tight binding. In contrast FKBP8 failed to bind intact Hsp70. The PPIase domain was not essential for the interaction with Hsp90 and binding was completely encompassed by the TPR domain alone. The conformation adopted by Hsp90 peptides, containing the conserved MEEVD motif, in the crystal structure were similar to that seen for the TPR domains of CHIP, AIP and Tah1...
2017: PloS One
https://www.readbyqxmd.com/read/28079882/stability-of-the-cancer-target-ddias-is-regulated-by-the-chip-hsp70-pathway-in-lung-cancer-cells
#6
Kyoung-Jae Won, Joo-Young Im, Bo-Kyung Kim, Hyun Seung Ban, Young-Jin Jung, Kyeong Eun Jung, Misun Won
DNA damage-induced apoptosis suppressor (DDIAS) rescues lung cancer cells from apoptosis in response to DNA damage. DDIAS is transcriptionally activated by NFATc1 and EGF-mediated ERK5/MEF2B, leading to cisplatin resistance and cell invasion. Therefore, DDIAS is suggested as a therapeutic target for lung cancer. Here, we report that DDIAS stability is regulated by E3 U-box ubiquitin ligase carboxyl terminus of HSP70-interacting protein (CHIP)-mediated proteasomal degradation. We first isolated CHIP as an interacting partner of DDIAS by yeast two-hybrid screening...
January 12, 2017: Cell Death & Disease
https://www.readbyqxmd.com/read/28053100/heat-shock-protein-90-ensures-efficient-mumps-virus-replication-by-assisting-with-viral-polymerase-complex-formation
#7
Hiroshi Katoh, Toru Kubota, Yuichiro Nakatsu, Maino Tahara, Minoru Kidokoro, Makoto Takeda
Paramyxoviral RNAs are synthesized by a viral RNA-dependent RNA polymerase (RdRp) consisting of the large (L) protein and its cofactor phosphoprotein (P protein). The L protein is a multifunctional protein that catalyzes RNA synthesis, mRNA capping, and mRNA polyadenylation. Growing evidence shows that the stability of several paramyxovirus L proteins is regulated by heat shock protein 90 (Hsp90). In this study, we demonstrated that Hsp90 activity was important for mumps virus (MuV) replication. The Hsp90 activity was required for L-protein stability and activity because an Hsp90-specific inhibitor, 17-allylamino-17-demethoxygeldanamycin (17-AAG), destabilized the MuV L protein and suppressed viral RNA synthesis...
March 15, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28042827/bag2-interferes-with-chip-mediated-ubiquitination-of-hsp72
#8
Bianca Schönbühler, Verena Schmitt, Heike Huesmann, Andreas Kern, Martin Gamerdinger, Christian Behl
The maintenance of cellular proteostasis is dependent on molecular chaperones and protein degradation pathways. Chaperones facilitate protein folding, maturation, and degradation, and the particular fate of a misfolded protein is determined by the interaction of chaperones with co-chaperones. The co-factor CHIP (C-terminus of HSP70-inteacting protein, STUB1) ubiquitinates chaperone substrates and directs proteins to the cellular degradation systems. The activity of CHIP is regulated by two co-chaperones, BAG2 and HSPBP1, which are potent inhibitors of the E3 ubiquitin ligase activity...
December 30, 2016: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/27863257/unraveling-the-chip-hsp70-complex-as-an-information-processor-for-protein-quality-control
#9
REVIEW
Jamie VanPelt, Richard C Page
The CHIP:Hsp70 complex stands at the crossroads of the cellular protein quality control system. Hsp70 facilitates active refolding of misfolded client proteins, while CHIP directs ubiquitination of misfolded client proteins bound to Hsp70. The direct competition between CHIP and Hsp70 for the fate of misfolded proteins leads to the question: how does the CHIP:Hsp70 complex execute triage decisions that direct misfolded proteins for either refolding or degradation? The current body of literature points toward action of the CHIP:Hsp70 complex as an information processor that takes inputs in the form of client folding state, dynamics, and posttranslational modifications, then outputs either refolded or ubiquitinated client proteins...
February 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/27852853/coat-protein-regulation-by-ck2-cpip-hsp70-and-chip-is-required-for-potato-virus-a-replication-and-coat-protein-accumulation
#10
Andres Lõhmus, Anders Hafrén, Kristiina Mäkinen
We demonstrate here that both coat protein (CP) phosphorylation by protein kinase CK2 and a chaperone system formed by two heat shock proteins, CP-interacting protein (CPIP) and heat shock protein 70 (HSP70), are essential for potato virus A (PVA; genus Potyvirus) replication and that all these host proteins have the capacity to contribute to the level of PVA CP accumulation. An E3 ubiquitin ligase called carboxyl terminus Hsc70-interacting protein (CHIP), which may participate in the CPIP-HSP70-mediated CP degradation, is also needed for robust PVA gene expression...
February 1, 2017: Journal of Virology
https://www.readbyqxmd.com/read/27809308/doxorubicin-attenuates-chip-guarded-hsf1-nuclear-translocation-and-protein-stability-to-trigger-igf-iir-dependent-cardiomyocyte-death
#11
Chih-Yang Huang, Wei-Wen Kuo, Jeng-Fan Lo, Tsung-Jung Ho, Pei-Ying Pai, Shu-Fen Chiang, Pei-Yu Chen, Fu-Jen Tsai, Chang-Hai Tsai, Chih-Yang Huang
Doxorubicin (DOX) is one of the most effective antitumor drugs, but its cardiotoxicity has been a major concern for its use in cancer therapy for decades. Although DOX-induced cardiotoxicity has been investigated, the underlying mechanisms responsible for this cardiotoxicity have not been completely elucidated. Here, we found that the insulin-like growth factor receptor II (IGF-IIR) apoptotic signaling pathway was responsible for DOX-induced cardiotoxicity via proteasome-mediated heat shock transcription factor 1 (HSF1) degradation...
November 3, 2016: Cell Death & Disease
https://www.readbyqxmd.com/read/27787517/parp1-regulates-the-protein-stability-and-proapoptotic-function-of-hipk2
#12
Jong-Ryoul Choi, Ki Soon Shin, Cheol Yong Choi, Shin Jung Kang
Homeodomain-interacting protein kinase 2 (HIPK2) is a nuclear serine/threonine kinase that functions in DNA damage response and development. In the present study, we propose that the protein stability and proapoptotic function of HIPK2 are regulated by poly(ADP-ribose) polymerase 1 (PARP1). We present evidence indicating that PARP1 promotes the proteasomal degradation of HIPK2. The tryptophan-glycine-arginine (WGR) domain of PARP1 was necessary and sufficient for the promotion of HIPK2 degradation independently of the PARP1 enzymatic activity...
October 27, 2016: Cell Death & Disease
https://www.readbyqxmd.com/read/27733512/recognition-of-enzymes-lacking-bound-cofactor-by-protein-quality-control
#13
Adrián Martínez-Limón, Marion Alriquet, Wei-Han Lang, Giulia Calloni, Ilka Wittig, R Martin Vabulas
Protein biogenesis is tightly linked to protein quality control (PQC). The role of PQC machinery in recognizing faulty polypeptides is becoming increasingly understood. Molecular chaperones and cytosolic and vacuolar degradation systems collaborate to detect, repair, or hydrolyze mutant, damaged, and mislocalized proteins. On the other hand, the contribution of PQC to cofactor binding-related enzyme maturation remains largely unexplored, although the loading of a cofactor represents an all-or-nothing transition in regard to the enzymatic function and thus must be surveyed carefully...
October 25, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/27709416/-1-h-15-n-and-13-c-resonance-assignments-for-free-and-ieevd-peptide-bound-forms-of-the-tetratricopeptide-repeat-domain-from-the-human-e3-ubiquitin-ligase-chip
#14
Huaqun Zhang, Cameron McGlone, Matthew M Mannion, Richard C Page
The ubiquitin ligase CHIP catalyzes covalent attachment of ubiquitin to unfolded proteins chaperoned by the heat shock proteins Hsp70/Hsc70 and Hsp90. CHIP interacts with Hsp70/Hsc70 and Hsp90 by binding of a C-terminal IEEVD motif found in Hsp70/Hsc70 and Hsp90 to the tetratricopeptide repeat (TPR) domain of CHIP. Although recruitment of heat shock proteins to CHIP via interaction with the CHIP-TPR domain is well established, alterations in structure and dynamics of CHIP upon binding are not well understood...
April 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/27475501/the-e3-ubiquitin-ligase-chip-selectively-regulates-mutant-epidermal-growth-factor-receptor-by-ubiquitination-and-degradation
#15
Chaeuk Chung, Geon Yoo, Tackhoon Kim, Dahye Lee, Choong-Sik Lee, Hye Rim Cha, Yeon Hee Park, Jae Young Moon, Sung Soo Jung, Ju Ock Kim, Jae Cheol Lee, Sun Young Kim, Hee Sun Park, Myoungrin Park, Dong Il Park, Dae-Sik Lim, Kang Won Jang, Jeong Eun Lee
Somatic mutation in the tyrosine kinase domain of epidermal growth factor receptor (EGFR) is a decisive factor for the therapeutic response to EGFR tyrosine kinase inhibitors (EGFR-TKIs) in lung adenocarcinoma. The stability of mutant EGFR is maintained by various regulators, including heat shock protein 90 (Hsp90). The C terminus of Hsc70-interacting protein (CHIP) is a Hsp70/Hsp90 co-chaperone and exhibits E3 ubiquitin ligase activity. The high-affinity Hsp90-CHIP complex recognizes and selectively regulates their client proteins...
October 14, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27443248/e3-ubiquitin-ligase-chip-interacts-with-c-type-lectin-like-receptor-clec-2-and-promotes-its-ubiquitin-proteasome-degradation
#16
Miaomiao Shao, Lili Li, Shushu Song, Weicheng Wu, Peike Peng, Caiting Yang, Mingming Zhang, Fangfang Duan, Dongwei Jia, Jie Zhang, Hao Wu, Ran Zhao, Lan Wang, Yuanyuan Ruan, Jianxin Gu
C-type lectin-like receptor 2 (CLEC-2) was originally identified as a member of non-classical C-type lectin-like receptors in platelets and immune cells. Activation of CLEC-2 is involved in thrombus formation, lymphatic/blood vessel separation, platelet-mediated tumor metastasis and immune response. Nevertheless, the regulation of CLEC-2 expression is little understood. In this study, we identified that the C terminus of Hsc70-interacting protein (CHIP) interacted with CLEC-2 by mass spectrometry analysis, and CHIP decreased the protein expression of CLEC-2 through lysine-48-linked ubiquitination and proteasomal degradation...
October 2016: Cellular Signalling
https://www.readbyqxmd.com/read/27392029/chip-involves-in-non-small-cell-lung-cancer-prognosis-through-vegf-pathway
#17
Qian Tingting, Wang Jiao, Wang Qingfeng, Liu Yancheng, Y U Shijun, Wang Zhaoqi, Sun Dongmei, Wang ShiLong
AIM: CHIP (c-terminal Hsp70-interacting protein) is an E3 ligase playing vital roles in various cancers. The VEGF pathway has become an important therapeutic target in non-small cell lung cancer (NSCLC). However, little is known about the role of CHIP and the relationship between CHIP and VEGF-VEGFR2 (VEGF receptor 2) pathway in NSCLC. In this study we aimed to investigate the clinical function of CHIP in NSCLC and explore the relevant regulatory mechanism. METHODS: QRT-PCR was performed to detect CHIP expression in NSCLC tissues...
October 2016: Biomedicine & Pharmacotherapy, Biomédecine & Pharmacothérapie
https://www.readbyqxmd.com/read/27342662/chip-promotes-thyroid-cancer-proliferation-via-activation-of-the-mapk-and-akt-pathways
#18
Li Zhang, Lianyong Liu, Xiaohua He, Yunling Shen, Xuerong Liu, Jing Wei, Fang Yu, Jianqing Tian
The carboxyl terminus of Hsp70-interacting protein (CHIP) is a U box-type ubiquitin ligase that plays crucial roles in various biological processes, including tumor progression. To date, the functional mechanism of CHIP in thyroid cancer remains unknown. Here, we obtained evidence of upregulation of CHIP in thyroid cancer tissues and cell lines. CHIP overexpression markedly enhanced thyroid cancer cell viability and colony formation in vitro and accelerated tumor growth in vivo. Conversely, CHIP knockdown impaired cell proliferation and tumor growth...
August 26, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27323684/protection-against-doxorubicin-induced-myocardial-dysfunction-in-mice-by-cardiac-specific-expression-of-carboxyl-terminus-of-hsp70-interacting-protein
#19
Lei Wang, Tian-Peng Zhang, Yuan Zhang, Hai-Lian Bi, Xu-Min Guan, Hong-Xia Wang, Xia Wang, Jie Du, Yun-Long Xia, Hui-Hua Li
Carboxyl terminus of Hsp70-interacting protein (CHIP) is a critical ubiquitin ligase/cochaperone to reduce cardiac oxidative stress, inflammation, cardiomyocyte apoptosis and autophage etc. However, it is unclear whether overexpression of CHIP in the heart would exert protective effects against DOX-induced cardiomyopathy. Cardiac-specific CHIP transgenic (CHIP-TG) mice and the wild-type (WT) littermates were treated with DOX or saline. DOX-induced cardiac atrophy, dysfunction, inflammation, oxidative stress and cardiomyocyte apoptosis were significantly attenuated in CHIP-TG mice...
2016: Scientific Reports
https://www.readbyqxmd.com/read/27178152/chip-mediates-down-regulation-of-nucleobindin-1-in-preosteoblast-cell-line-models
#20
Fuying Xue, Yanping Wu, Xinghui Zhao, Taoran Zhao, Ying Meng, Zhanzhong Zhao, Junwei Guo, Wei Chen
Nucleobindin-1 (NUCB1), also known as Calnuc, is a highly conserved, multifunctional protein widely expressed in tissues and cells. It contains two EF-hand motifs which have been shown to play a crucial role in binding Ca(2+) ions. In this study, we applied comparative two-dimensional gel electrophoresis to characterize differentially expressed proteins in HA-CHIP over-expressed and endogenous CHIP depleted MC3T3-E1 stable cell lines, identifying NUCB1 as a novel CHIP/Stub1 targeted protein. NUCB1 interacts with and is down-regulated by CHIP by both proteasomal dependent and independent pathways, suggesting that CHIP-mediated down-regulation of nucleobindin-1 might play a role in osteoblast differentiation...
2016: Cellular Signalling
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