keyword
MENU ▼
Read by QxMD icon Read
search

hsp70 interacting protein

keyword
https://www.readbyqxmd.com/read/28903051/features-of-the-chaperone-cellular-network-revealed-through-systematic-interaction-mapping
#1
Kamran Rizzolo, Jennifer Huen, Ashwani Kumar, Sadhna Phanse, James Vlasblom, Yoshito Kakihara, Hussein A Zeineddine, Zoran Minic, Jamie Snider, Wen Wang, Carles Pons, Thiago V Seraphim, Edgar Erik Boczek, Simon Alberti, Michael Costanzo, Chad L Myers, Igor Stagljar, Charles Boone, Mohan Babu, Walid A Houry
A comprehensive view of molecular chaperone function in the cell was obtained through a systematic global integrative network approach based on physical (protein-protein) and genetic (gene-gene or epistatic) interaction mapping. This allowed us to decipher interactions involving all core chaperones (67) and cochaperones (15) of Saccharomyces cerevisiae. Our analysis revealed the presence of a large chaperone functional supercomplex, which we named the naturally joined (NAJ) chaperone complex, encompassing Hsp40, Hsp70, Hsp90, AAA+, CCT, and small Hsps...
September 12, 2017: Cell Reports
https://www.readbyqxmd.com/read/28902917/hsp70-j-protein-machinery-from-glossina-morsitans-morsitans-vector-of-african-trypanosomiasis
#2
Stephen J Bentley, Aileen Boshoff
Tsetse flies (Glossina spp.) are the sole vectors of the protozoan parasites of the genus Trypanosoma, the causative agents of African Trypanosomiasis. Species of Glossina differ in vector competence and Glossina morsitans morsitans is associated with transmission of Trypanosoma brucei rhodesiense, which causes an acute and often fatal form of African Trypanosomiasis. Heat shock proteins are evolutionarily conserved proteins that play critical roles in proteostasis. The activity of heat shock protein 70 (Hsp70) is regulated by interactions with its J-protein (Hsp40) co-chaperones...
2017: PloS One
https://www.readbyqxmd.com/read/28894176/overlapping-and-specific-functions-of-the-hsp104-n-domain-define-its-role-in-protein-disaggregation
#3
Jungsoon Lee, Nuri Sung, Jonathan M Mercado, Corey F Hryc, Changsoo Chang, Sukyeong Lee, Francis T F Tsai
Hsp104 is a ring-forming protein disaggregase that rescues stress-damaged proteins from an aggregated state. To facilitate protein disaggregation, Hsp104 cooperates with Hsp70 and Hsp40 chaperones (Hsp70/40) to form a bi-chaperone system. How Hsp104 recognizes its substrates, particularly the importance of the N domain, remains poorly understood and multiple, seemingly conflicting mechanisms have been proposed. Although the N domain is dispensable for protein disaggregation, it is sensitive to point mutations that abolish the function of the bacterial Hsp104 homolog in vitro, and is essential for curing yeast prions by Hsp104 overexpression in vivo...
September 11, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28893371/heterogeneous-interaction-network-of-yeast-prions-and-remodeling-factors-detected-in-live-cells
#4
Chan-Gi Pack, Yuji Inoue, Takashi Higurashi, Shigeko Kawai-Noma, Daigo Hayashi, Elizabeth Craig, Hideki Taguchi
Budding yeast has dozens of prions, which are mutually dependent on each other for the de novo prion formation. In addition to the interactions among prions, transmissions of prions are strictly dependent on two chaperone systems: the Hsp104 and the Hsp70/Hsp40 (J-protein) systems, both of which cooperatively remodel the prion aggregates to ensure the multiplication of prion entities. Since it has been postulated that prions and the remodeling factors constitute complex networks in cells, a quantitative approach to describe the interactions in live cells would be required...
September 12, 2017: BMB Reports
https://www.readbyqxmd.com/read/28882200/fe-s-cluster-hsp70-chaperones-the-atpase-cycle-and-protein-interactions
#5
Rafal Dutkiewicz, Malgorzata Nowak, Elizabeth A Craig, Jaroslaw Marszalek
Hsp70 chaperones and their obligatory J-protein cochaperones function together in many cellular processes. Via cycles of binding to short stretches of exposed amino acids on substrate proteins, Hsp70/J-protein chaperones not only facilitate protein folding but also drive intracellular protein transport, biogenesis of cellular structures, and disassembly of protein complexes. The biogenesis of iron-sulfur (Fe-S) clusters is one of the critical cellular processes that require Hsp70/J-protein action. Fe-S clusters are ubiquitous cofactors critical for activity of proteins performing diverse functions in, for example, metabolism, RNA/DNA transactions, and environmental sensing...
2017: Methods in Enzymology
https://www.readbyqxmd.com/read/28878328/clec14a-hsp70-1a-interaction-regulates-hsp70-1a-induced-angiogenesis
#6
Jihye Jang, Mi Ra Kim, Taek-Keun Kim, Woo Ran Lee, Jong Heon Kim, Kyun Heo, Sukmook Lee
CLEC14a (C-type lectin domain family 14 member) is a tumor endothelial cell marker protein that is known to play an important role in tumor angiogenesis, but the basic molecular mechanisms underlying this function have not yet been clearly elucidated. In this study, using various proteomic tools, we isolated a 70-kDa protein that interacts with the C-type lectin-like domain of CLEC14a (CLEC14a-CTLD) and identified it as heat shock protein 70-1A (HSP70-1A). Co-immunoprecipitation showed that HSP70-1A and CLEC14a interact on endothelial cells...
September 6, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28860596/mapk1-of-leishmania-donovani-interacts-and-phosphorylates-hsp70-and-hsp90-subunits-of-foldosome-complex
#7
Pavneet Kaur, Mansi Garg, Antje Hombach-Barrigah, Joachim Clos, Neena Goyal
MAP kinases (MAPK) are the most downstream kinases in signal transduction cascades and regulate critical cellular activities such as cell proliferation, differentiation, mortality, stress response, and apoptosis. The Leishmania donovani MAPK1 (LdMAPK1) is involved in parasite viability and drug resistance, but its substrates have not been identified yet. Aiming to identify the possible targets(s) of LdMAPK1, we sought to isolate interacting partners by co-immunoprecipitation, gel electrophoresis and mass spectrometry...
August 31, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28859986/kribb11-accelerates-mcl-1-degradation-through-an-hsf1-independent-mule-dependent-pathway-in-a549-non-small-cell-lung-cancer-cells
#8
Min-Jung Kang, Hye Hyeon Yun, Jeong-Hwa Lee
The Bcl-2 family protein, Mcl-1 is known to have anti-apoptotic functions, and depletion of Mcl-1 by cellular stresses favors the apoptotic process. Moreover, Mcl-1 levels are frequently increased in various cancer cells, including non-small cell lung cancer (NSCLC), and is implicated in resistance to conventional chemotherapy and in cancer metastasis. In this study, we demonstrated that KRIBB11 accelerates the proteasomal degradation of Mcl-1 in the NSCLC cell line, A549. While KRIBB11 is an inhibitor of HSF1, we found that KRIBB11 induced Mcl-1 degradation in an HSF1-independent manner...
August 29, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28833766/conformational-heterogeneity-in-the-hsp70-chaperone-substrate-ensemble-identified-from-analysis-of-nmr-detected-titration-data
#9
Ashok Sekhar, Jayashree Nagesh, Rina Rosenzweig, Lewis E Kay
The Hsp70 chaperone system plays a critical role in cellular homeostasis by binding to client protein molecules. We have recently shown by methyl-TROSY NMR methods that the Escherichia coli Hsp70, DnaK, can form multiple bound complexes with a small client protein, hTRF1. In an effort to characterize the interactions further we report here the results of an NMR-based titration study of hTRF1 and DnaK, where both molecular components are monitored simultaneously, leading to a binding model. A central finding is the formation of a previously undetected 3:1 hTRF1-DnaK complex, suggesting that under heat shock conditions, DnaK might be able to protect cytosolic proteins whose net concentrations would exceed that of the chaperone...
August 19, 2017: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/28819167/artificial-dnaj-protein-for-protein-production-and-conformational-diseases
#10
Akinori Hishiya, Keizo Koya
For secreted proteins, proper protein folding is essential not only for biological function but also for secretion itself. Proteins with folding problems are trapped in the endoplasmic reticulum (ER) and are eventually degraded in the cytoplasm. In this study, we exploited co-expression of an artificial fusion protein, based on the sequence of a DnaJ protein, which could interact as co-chaperones in the Hsp70-based protein-folding system, with target recombinant secreted proteins to enhance their production and secretion...
August 17, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28819163/fusion-protein-analysis-reveals-the-precise-regulation-between-hsp70-and-hsp100-during-protein-disaggregation
#11
Sayaka Hayashi, Yosuke Nakazaki, Kei Kagii, Hiromi Imamura, Yo-Hei Watanabe
ClpB, a bacterial Hsp100, is a ring-shaped AAA+ chaperone that can reactivate aggregated proteins in cooperation with DnaK, a bacterial Hsp70, and its co-factors. ClpB subunits comprise two AAA+ modules with an interstitial rod-shaped M-domain. The M-domain regulates ClpB ATPase activity and interacts directly with the DnaK nucleotide-binding domain (NBD). Here, to clarify how these functions contribute to the disaggregation process, we constructed ClpB, DnaK, and aggregated YFP fusion proteins in various combinations...
August 17, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28792733/crohn-s-disease-variants-of-nod2-are-stabilized-by-the-critical-contact-region-of-hsp70
#12
Amy K Schaefer, Hannah C Wastyk, Vishnu Mohanan, Ching-Wen Hou, Mackenzie L Lauro, James E Melnyk, Jason M Burch, Catherine L Grimes
Nod2 is a cytosolic, innate immune receptor responsible for binding to bacterial cell wall fragments such as muramyl dipeptide (MDP). Upon binding, subsequent downstream activation of the NF-κB pathway leads to an immune response. Nod2 mutations are correlated with an increased susceptibility to Crohn's disease (CD) and ultimately result in a misregulated immune response. Previous work had demonstrated that Nod2 interacts with and is stabilized by the molecular chaperone Hsp70. In this work, it is shown using purified protein and in vitro biochemical assays that the critical Nod2 CD mutations (G908R, R702W, and 1007fs) preserve the ability to bind bacterial ligands...
August 29, 2017: Biochemistry
https://www.readbyqxmd.com/read/28771464/two-chaperones-locked-in-an-embrace-structure-and-function-of-the-ribosome-associated-complex-rac
#13
REVIEW
Ying Zhang, Irmgard Sinning, Sabine Rospert
Chaperones, which assist protein folding are essential components of every living cell. The yeast ribosome-associated complex (RAC) is a chaperone that is highly conserved in eukaryotic cells. The RAC consists of the J protein Zuo1 and the unconventional Hsp70 homolog Ssz1. The RAC heterodimer stimulates the ATPase activity of the ribosome-bound Hsp70 homolog Ssb, which interacts with nascent polypeptide chains to facilitate de novo protein folding. In addition, the RAC-Ssb system is required to maintain the fidelity of protein translation...
August 3, 2017: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/28770685/insulin-igf-signaling-and-life-history-traits-in-response-to-food-availability-and-perceived-density-in-the-cnidarian-hydra-vulgaris
#14
Flóra Sebestyén, Szilárd Póliska, Rita Rácz, Judit Bereczki, Kinga Lénárt, Zoltán Barta, Ádám Z Lendvai, Jácint Tökölyi
Insulin/insulin-like growth factor signaling (IIS) is thought to be a central mediator of life history traits, but the generality of its role is not clear. Here, we investigated mRNA expression levels of three insulin-like peptide genes, the insulin-like receptor htk7, as well as several antioxidant genes, and the heat-shock protein hsp70 in the freshwater cnidarian Hydra vulgaris. Hydra polyps were exposed to a combination of different levels of food and perceived population density to manipulate life history traits (asexual reproduction and oxidative stress tolerance)...
August 2017: Zoological Science
https://www.readbyqxmd.com/read/28769758/the-role-of-bip-retrieval-by-the-kdel-receptor-in-the-early-secretory-pathway-and-its-effect-on-protein-quality-control-and-neurodegeneration
#15
REVIEW
Hisayo Jin, Mari Komita, Tomohiko Aoe
Protein quality control in the early secretory pathway is a ubiquitous eukaryotic mechanism for adaptation to endoplasmic reticulum (ER) stress. An ER molecular chaperone, immunoglobulin heavy chain-binding protein (BiP), is one of the essential components in this process. BiP interacts with nascent proteins to facilitate their folding. BiP also plays an important role in preventing aggregation of misfolded proteins and regulating the ER stress response when cells suffer various injuries. BiP is a member of the 70-kDa heat shock protein (HSP70) family of molecular chaperones that resides in the ER...
2017: Frontiers in Molecular Neuroscience
https://www.readbyqxmd.com/read/28757353/osmotic-and-heat-stress-dependent-regulation-of-mlk4%C3%AE-and-mlk3-by-the-chip-e3-ligase-in-ovarian-cancer-cells
#16
Natalya A Blessing, Srimathi Kasturirangan, Evan M Zink, April L Schroyer, Deborah N Chadee
Mixed Lineage Kinase 3 (MLK3), a member of the MLK subfamily of protein kinases, is a mitogen-activated protein (MAP) kinase kinase kinase (MAP3K) that activates MAPK signalling pathways and regulates cellular responses such as proliferation, invasion and apoptosis. MLK4β, another member of the MLK subfamily, is less extensively studied, and the regulation of MLK4β by stress stimuli is not known. In this study, the regulation of MLK4β and MLK3 by osmotic stress, thermostress and heat shock protein 90 (Hsp90) inhibition was investigated in ovarian cancer cells...
November 2017: Cellular Signalling
https://www.readbyqxmd.com/read/28754691/the-hsp70-interdomain-linker-is-a-dynamic-switch-that-enables-allosteric-communication-between-two-structured-domains
#17
Charles A English, Woody Sherman, Wenli Meng, Lila M Gierasch
Hsp70 molecular chaperones play key roles in cellular protein homeostasis by binding to exposed hydrophobic regions of incompletely folded or aggregated proteins. This crucial Hsp70 function relies on allosteric communication between two well-structured domains: an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD), which are tethered by an interdomain linker. ATP or ADP binding to the NBD alters the substrate-binding affinity of the SBD, triggering functionally essential cycles of substrate binding and release...
September 8, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28745541/chaperone-proteins-as-single-component-reagents-to-assess-antibody-nonspecificity
#18
Ryan L Kelly, James C Geoghegan, Jared Feldman, Tushar Jain, Monique Kauke, Doris Le, Jessie Zhao, K Dane Wittrup
Early stage assays that evaluate monoclonal antibody drug-like properties serve as valuable tools for selection of lead candidates. One liability for clinical development, off-target reactivity, is often assessed by binding to a mixture or panel of noncognate proteins. While robust, these mixes are often ill-defined, and can suffer from issues such as lot-to-lot variability. In this study, we discovered in immunoprecipitation experiments that certain chaperones are present in one of these mixtures; we then explored the use of recombinant chaperone proteins as well-characterized agents to predict antibody nonspecificity...
July 26, 2017: MAbs
https://www.readbyqxmd.com/read/28737514/bag3-plays-a-central-role-in-proteostasis-in-the-heart
#19
Wataru Mizushima, Junichi Sadoshima
Proteinopathies are characterized by the accumulation of misfolded proteins, which ultimately interfere with normal cell function. While neurological diseases, such as Huntington disease and Alzheimer disease, are well-characterized proteinopathies, cardiac diseases have recently been associated with alterations in proteostasis. In this issue of the JCI, Fang and colleagues demonstrate that mice with cardiac-specific deficiency of the co-chaperone protein BCL2-associated athanogene 3 (BAG3) develop dilated cardiomyopathy that is associated with a destabilization of small HSPs as the result of a disrupted interaction between BAG3 and HSP70...
August 1, 2017: Journal of Clinical Investigation
https://www.readbyqxmd.com/read/28737513/loss-of-function-mutations-in-co-chaperone-bag3-destabilize-small-hsps-and-cause-cardiomyopathy
#20
Xi Fang, Julius Bogomolovas, Tongbin Wu, Wei Zhang, Canzhao Liu, Jennifer Veevers, Matthew J Stroud, Zhiyuan Zhang, Xiaolong Ma, Yongxin Mu, Dieu-Hung Lao, Nancy D Dalton, Yusu Gu, Celine Wang, Michael Wang, Yan Liang, Stephan Lange, Kunfu Ouyang, Kirk L Peterson, Sylvia M Evans, Ju Chen
Defective protein quality control (PQC) systems are implicated in multiple diseases. Molecular chaperones and co-chaperones play a central role in functioning PQC. Constant mechanical and metabolic stress in cardiomyocytes places great demand on the PQC system. Mutation and downregulation of the co-chaperone protein BCL-2-associated athanogene 3 (BAG3) are associated with cardiac myopathy and heart failure, and a BAG3 E455K mutation leads to dilated cardiomyopathy (DCM). However, the role of BAG3 in the heart and the mechanisms by which the E455K mutation leads to DCM remain obscure...
August 1, 2017: Journal of Clinical Investigation
keyword
keyword
55480
1
2
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read
×

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"