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2015, 2nd edition., Advances in applied mathematics, ISBN 9781482251029, xvii, 667
Book
1999, 1, Mechanical engineering, ISBN 0824719417, Volume 119., x, 469
Book
2013, ISBN 9781107025172, Volume 9781107025172, xiv, 400 pages
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2011, Chapman & Hall/CRC applied mathematics and nonlinear science series., ISBN 9781439840085, xxv, 356 p.4.
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Biomedical Journal, ISSN 2319-4170, 05/2013, Volume 36, Issue 3, pp. 106 - 117
Hsp90 | conformational cycle | clients | posttranslational modifications | ATPase | co-chaperones | Animals | HSP90 Heat-Shock Proteins - antagonists & inhibitors | HSP90 Heat-Shock Proteins - physiology | Humans | HSP90 Heat-Shock Proteins - chemistry | Protein Conformation | Protein Processing, Post-Translational | Molecular Chaperones - physiology | Signal transduction | Antibiotics | Protein folding | Breast cancer | Kinases | Machinery | Binding sites | Index Medicus | Hsp90 can be secreted as well and it promotes tumor invasiveness. Blocking the secreted Hsp90 led to a significant inhibition of tumor metastasis. Structure of Hsp90 Top Structurally | nucleotide binding is not the only determinant for Hsp90 conformation. The interaction with co-chaperones and client protein also influences the conformational rearrangement of Hsp90. | p23/Sba1 | eNOS | in which the ATP lid is closed but the N-domains are still open. The N-terminal dimerization leads to the formation of the second intermediate state (I2) | while Hsp90β is constitutively expressed. Hsp90 analogues also exist in other cellular compartments such as Grp94 in the endoplasmic reticulum | the M-domain contributes to the interaction sites for client proteins and some co-chaperones. The C-domain is essential for the dimerization of Hsp90. Interestingly | Hsp90 works together with a large group of cofactors | the activation of its client protein | MutL (GHKL) domain ATPases | Therefore | Binding of Aha1 induces a partially closed Hsp90 conformation and accelerates the progression of the ATPase cycle dramatically. | Different from other well-known molecular chaperone like Hsp70 and GroEL/ES | Interestingly | 113 | which acts as a core modulator in plant immunity. During the recruitment and activation of NLRs | more than 200 Hsp90 client proteins have been identified (see http://www.picard.ch/downloads/Hsp90interactors.pdf ). Besides the well-studied clients such as protein kinases and SHRs | 115 | termed co-chaperones. Co-chaperones form defined binary or ternary complexes with Hsp90 | 116 | Our understanding of the Hsp90 machinery has been greatly advanced by research of the last decades. However | 118 | Function and Regulation of the Hsp90 Machinery. Biomed J 2013;36:106-17 How to cite this URL: Li J | leading to an asymmetric intermediate complex. Hsp90 adopts the ATPase-active (closed) conformation after binding of ATP. p23/Sba1 stabilizes the closed state of Hsp90 | and protein degradation. Interestingly | the lid segment is very flexible | and the NLR protein may dissociate from Hsp90. Hsp90 complexes in RNA processing Recent studies showed that Hsp90 is also involved in the assembly of small nucleolar ribonucleoproteins (snoRNPs) and RNA polymerase. | 15 | the lid segment promotes ATP hydrolysis. Once ATP is hydrolyzed | with 1 min–1 for yeast Hsp90 and 0.1 min–1 for human Hsp90. | hyperphosphorylation also leads to a decreased Hsp90 activity. In yeast | although a TPR domain is present in Sgt1 as well | California | Germany Date of Submission 05-Sep-2012 Date of Acceptance 02-Nov-2012 Date of Web Publication 10-Jun-2013 Correspondence Address: Johannes Buchner Center for Integrated Protein Science | the M-domain in blue | which weakens the binding of Hop/Sti1 and promotes its exit from the complex. Potentially another PPIase (dashed line) associates to form the "late complex" together with Hsp90 and p23/Sba1. After the hydrolysis of ATP | posttranslational modifications of Hsp90 | and protein degradation | 125 | 5 | the protein phosphatase PP5 (yeast homologue Ppt1) | 6 | in eukaryotic Hsp90 | such as mitochondrial/chloroplast protein import (Tom70/Toc64) | 9 | In Ppt1 knockout strains | posttranslational modifications How to cite this article: Li J | Hsp90 is a homodimer and each protomer contains three flexibly linked regions | p23 is a conformation-specific co-chaperone which binds exclusively to the closed conformation of Hsp90. | 24 | viral infection | 27 | Fkbp51 | They regulate the function of Hsp90 in different ways such as inhibition and activation of the ATPase of Hsp90 as well as recruitment of specific client proteins to the cycle. Interestingly | such as double-stranded DNA protein kinase | in which the ATP lid is closed but the N-domains are still open. Then | 132 | one of the most abundant and conserved molecular chaperones | and the C-domain in orange. Click here to view Conformational dynamics of Hsp90 Top Hsp90 is a weak ATPase and the turnover rates are very low |