GRP94: an HSP90-like protein specialized for protein folding and quality control in the Endoplasmic Reticulum
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TLDR
Glucose-regulated protein 94 is the HSP90-like protein in the lumen of the endoplasmic reticulum and therefore it chaperones secreted and membrane proteins and the basis for this selectivity remains obscure.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 2012-03-01 and is currently open access. It has received 335 citations till now. The article focuses on the topics: Co-chaperone & Chaperone (protein).read more
Citations
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Journal ArticleDOI
Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential
TL;DR: The glucose-regulated proteins are found and regulation are described, as well as their biological functions in cancer and promising agents that use or target the GRPs are developed, and their efficacy as anticancer therapeutics is discussed.
Journal ArticleDOI
The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
TL;DR: This manuscript will review the general structure, regulation and function of HSP90 family and their potential role in pathophysiology.
Journal ArticleDOI
The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases.
Rachel E. Lackie,Andrzej Maciejewski,Valeriy G. Ostapchenko,Jose Marques-Lopes,Wing-Yiu Choy,Martin L. Duennwald,Vania F. Prado,Marco A. M. Prado +7 more
TL;DR: The role of intracellular and extracellular STI1 and the Hsp70/Hsp90 chaperone network in mechanisms underlying protein misfolding in neurodegenerative diseases, with particular focus on AD is discussed.
Book ChapterDOI
Hsp90: Structure and Function.
TL;DR: The focus of this review is the structural and mechanistic studies which have been performed in order to understand how this important chaperone acts on a wide variety of different proteins (its client proteins) and cellular processes.
Journal ArticleDOI
Role of the unfolded protein response, GRP78 and GRP94 in organ homeostasis.
Genyuan Zhu,Amy S. Lee +1 more
TL;DR: This review highlights recent progress towards the understanding of the role of the UPR and two major GRPs in regulating homeostasis of organs arising from the endoderm, mesoderm and ectoderm.
References
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Journal ArticleDOI
Signal integration in the endoplasmic reticulum unfolded protein response
David Ron,Peter Walter +1 more
TL;DR: Together, at least three mechanistically distinct arms of the UPR regulate the expression of numerous genes that function within the secretory pathway but also affect broad aspects of cell fate and the metabolism of proteins, amino acids and lipids.
Journal ArticleDOI
Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions
Chunaram Choudhary,Chanchal Kumar,Florian Gnad,Michael L. Nielsen,Michael Rehman,Tobias C. Walther,Jesper V. Olsen,Matthias Mann +7 more
TL;DR: A proteomic-scale analysis of protein acetylation suggests that it is an important biological regulatory mechanism and the regulatory scope of lysine acetylations is broad and comparable with that of other major posttranslational modifications.
Journal ArticleDOI
XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor
TL;DR: The transcription factor XBP1, a target of ATF6, is identified as a mammalian substrate of such an unconventional mRNA splicing system and it is shown that only the spliced form of X BP1 can activate the UPR efficiently.
Journal ArticleDOI
Molecular chaperones in cellular protein folding.
TL;DR: Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.
Journal ArticleDOI
Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes
Umut Ozcan,Qiong Cao,Erkan Yilmaz,Ann-Hwee Lee,Neal N. Iwakoshi,Esra Özdelen,Gurol Tuncman,Cem Z. Görgün,Laurie H. Glimcher,Gökhan S. Hotamisligil +9 more
TL;DR: It is shown that obesity causes endoplasmic reticulum (ER) stress, which leads to suppression of insulin receptor signaling through hyperactivation of c-Jun N-terminal kinase (JNK) and subsequent serine phosphorylation of insulin receptors substrate–1 (IRS-1).