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chip hsp70 interacting protein

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 12, 2016: Proceedings of the National Academy of Sciences of the United States of America
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...
October 5, 2016: Biomolecular NMR Assignments
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
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
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...
July 5, 2016: Biomedicine & Pharmacotherapy, Biomédecine & Pharmacothérapie
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
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
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...
August 2016: Cellular Signalling
Hyo Rim Ko, Yun Sil Chang, Won Soon Park, Jee-Yin Ahn
The different functions of the two isoforms of ErbB3 binding protein 1 (Ebp1), p48 and p42, have recently become the focus of interest as they reveal contradictory roles in cell growth promoting ability. The conformational change that crystal structure of p42 was shown to lack α helices at the amino-terminus present in p48 represents the differential binding partners and protein modifications of two Ebp1 isoforms. N-terminal specific phosphorylation by CDK2 and deregulation of the p53 tumor suppressor through specific interaction with HDM2 and Akt activation is postulated to contribute to p48-mediated tumorigenesis...
September 15, 2016: International Journal of Cancer. Journal International du Cancer
Jinho Seo, Eun-Woo Lee, Hyerim Sung, Daehyeon Seong, Yves Dondelinger, Jihye Shin, Manhyung Jeong, Hae-Kyung Lee, Jung-Hoon Kim, Su Yeon Han, Cheolju Lee, Je Kyung Seong, Peter Vandenabeele, Jaewhan Song
Receptor-interacting protein kinase 3 (RIPK3) functions as a key regulator of necroptosis. Here, we report that the RIPK3 expression level is negatively regulated by CHIP (carboxyl terminus of Hsp70-interacting protein; also known as STUB1) E3 ligase-mediated ubiquitylation. Chip(-/-) mouse embryonic fibroblasts and CHIP-depleted L929 and HT-29 cells exhibited higher levels of RIPK3 expression, resulting in increased sensitivity to necroptosis induced by TNF (also known as TNFα). These phenomena are due to the CHIP-mediated ubiquitylation of RIPK3, which leads to its lysosomal degradation...
March 2016: Nature Cell Biology
B Min, H Park, S Lee, Y Li, J-M Choi, J Y Lee, J Kim, Y D Choi, Y-G Kwon, H-W Lee, S-C Bae, C-O Yun, K C Chung
The multifunctional enzyme transglutaminase 2 (TG2) primarily catalyzes cross-linking reactions of proteins via (γ-glutamyl) lysine bonds. Several recent findings indicate that altered regulation of intracellular TG2 levels affects renal cancer. Elevated TG2 expression is observed in renal cancer. However, the molecular mechanism underlying TG2 degradation is not completely understood. Carboxyl-terminus of Hsp70-interacting protein (CHIP) functions as an ubiquitin E3 ligase. Previous studies reveal that CHIP deficiency mice displayed a reduced life span with accelerated aging in kidney tissues...
July 14, 2016: Oncogene
A Mendoza, D M Torrisi, S Sell, N C Cady, D A Lawrence
Biomarker discovery for early disease diagnosis is highly important. Of late, much effort has been made to analyze complex biological fluids in an effort to develop new markers specific for different cancer types. Recent advancements in label-free technologies such as surface plasmon resonance (SPR)-based biosensors have shown promise as a diagnostic tool since there is no need for labeling or separation of cells. Furthermore, SPR can provide rapid, real-time detection of antigens from biological samples since SPR is highly sensitive to changes in surface-associated molecular and cellular interactions...
January 21, 2016: Analyst
Vikram Narayan, Vivien Landré, Jia Ning, Lenka Hernychova, Petr Muller, Chandra Verma, Malcolm D Walkinshaw, Elizabeth A Blackburn, Kathryn L Ball
CHIP is a tetratricopeptide repeat (TPR) domain protein that functions as an E3-ubiquitin ligase. As well as linking the molecular chaperones to the ubiquitin proteasome system, CHIP also has a docking-dependent mode where it ubiquitinates native substrates, thereby regulating their steady state levels and/or function. Here we explore the effect of Hsp70 on the docking-dependent E3-ligase activity of CHIP. The TPR-domain is revealed as a binding site for allosteric modulators involved in determining CHIP's dynamic conformation and activity...
November 2015: Molecular & Cellular Proteomics: MCP
W Zhang, Z Liu, X Bao, Y Qin, A Taylor, F Shang, M Wu
Protein quality control (PQC) systems, including molecular chaperones and ubiquitin-proteasome pathway (UPP), plays an important role in maintaining intracellular protein homeostasis. Carboxyl terminus of Hsc70- interacting protein (CHIP) links the chaperone and UPPs, thus contributing to the repair or removal of damaged proteins. Over-expression of CHIP had previously been used to protect cells from environmental stress. In order to gain a more physiologic mechanism of the advantage conferred by CHIP, we induced a CHIP knockdown and monitored the ability of cells to cope with environmental stress...
2015: Current Molecular Medicine
Andrea F Gil Lorenzo, Valeria V Costantino, Martin López Appiolaza, Valeria Cacciamani, Maria E Benardon, Victoria Bocanegra, Patricia G Vallés
BACKGROUND: Angiotensin II/Angiotensin II type 1 receptor (AT1R) effects are dependent on ROS production stimulated by NADPH oxidase activation. Hsp70 regulates a diverse set of signaling pathways through their interactions with proteins. CHIP is a E3 ubiquitin ligase that targets proteins for polyubiquitination and degradation. AIM: We study whether Hsp70/CHIP contribute to the negative regulation of Nox4 after AT1R blockage. METHODS/RESULTS: Primary culture of proximal tubule epithelial cells (PTCs) from SHR and WKY were stimulated with Angiotensin II (AII) or treated with Losartan (L) or Losartan plus Angiotensin II (L+AII)...
2015: Cellular Physiology and Biochemistry
Yanfen Teng, Khosrow Rezvani, Mariella De Biasi
Neuronal nicotinic acetylcholine receptors (nAChRs) containing the α3 subunit are known for their prominent role in normal ganglionic transmission while their involvement in the mechanisms underlying nicotine addiction and smoking-related disease has been emerging only in recent years. The amount of information available on the maturation and trafficking of α3-containing nAChRs is limited. We previously showed that UBXN2A is a p97 adaptor protein that facilitates the maturation and trafficking of α3-containing nAChRs...
October 15, 2015: Biochemical Pharmacology
Chao Sun, Hai-long Li, Hai-rong Chen, Mei-lin Shi, Qing-hua Liu, Zhen-qiang Pan, Jin Bai, Jun-nian Zheng
CHIP (c-terminal Hsp70-interacting protein) is an E3 ligase which may play different roles in different cancers. The elucidation of the VHL-HIF-1α (hypoxia inducible factor-1α)-VEGF (vascular endothelial growth factor) pathway has led to the development of targeted therapy in renal cell carcinoma (RCC). However, little is known about the role of CHIP and the relationship between CHIP and VEGF-VEGFR2 (VEGF receptor 2) pathway in RCC. In this study, we found that the expression of CHIP was downregulated and significantly correlated with pT status (P = 0...
2015: Scientific Reports
Ye Jin, Li Zhou, Zhi-Yong Liang, Ke-Min Jin, Wei-Xun Zhou, Bao-Cai Xing
BACKGROUND: Many factors, including molecular ones, were demonstrated to be associated with long-term prognosis of hepatocellular carcinoma (HCC). Thus far, the expression and clinicopathologic and prognostic significance of the carboxyl terminus of Hsp70-interacting protein (CHIP) in B-type hepatitis virus (HBV)- related HCC remain unknown. MATERIALS AND METHODS: CHIP expression was detected by immunohistochemical staining of surgical samples from 79 patients with HCC with HBsAg positivity...
2015: Asian Pacific Journal of Cancer Prevention: APJCP
Jianmin Xie, Jieruo Gu
In patients with inflammatory arthritis, tumour necrosis factor (TNF)-α are overproduced in inflamed joints. This leads to local erosion of cartilage and bone, periarticular osteopenia, as well as osteoporosis. But less is known regarding the molecular mechanisms that mediate the effect of TNF-α on osteoblast function. The purpose of this study was to test that C terminus of Hsc70-interacting protein (CHIP) has a specific role in suppressing the osteogenic activity of osteoblasts under inflammatory conditions...
August 2015: Journal of Cellular and Molecular Medicine
Huaqun Zhang, Joseph Amick, Ritu Chakravarti, Stephanie Santarriaga, Simon Schlanger, Cameron McGlone, Michelle Dare, Jay C Nix, K Matthew Scaglione, Dennis J Stuehr, Saurav Misra, Richard C Page
The ubiquitin ligase CHIP plays an important role in cytosolic protein quality control by ubiquitinating proteins chaperoned by Hsp70/Hsc70 and Hsp90, thereby targeting such substrate proteins for degradation. We present a 2.91 Å resolution structure of the tetratricopeptide repeat (TPR) domain of CHIP in complex with the α-helical lid subdomain and unstructured tail of Hsc70. Surprisingly, the CHIP-TPR interacts with determinants within both the Hsc70-lid subdomain and the C-terminal PTIEEVD motif of the tail, exhibiting an atypical mode of interaction between chaperones and TPR domains...
March 3, 2015: Structure
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