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The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin. Nat Struct Mol Biol 15: 858–864 (2008)

by J Cuellar, J Martı́n-Benito, Scheres SH, R Sousa, F Moro
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The cytosolic chaperonin CCT/TRiC and cancer cell proliferation

by Chafika Boudiaf-benmammar, Thierry Cresteil, Ronald Melki - PLoS ONE
"... The molecular chaperone CCT/TRiC plays a central role in maintaining cellular proteostasis as it mediates the folding of the major cytoskeletal proteins tubulins and actins. CCT/TRiC is also involved in the oncoprotein cyclin E, the Von Hippel-Lindau tumour suppressor protein, cyclin B and p21ras fo ..."
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The molecular chaperone CCT/TRiC plays a central role in maintaining cellular proteostasis as it mediates the folding of the major cytoskeletal proteins tubulins and actins. CCT/TRiC is also involved in the oncoprotein cyclin E, the Von Hippel-Lindau tumour suppressor protein, cyclin B and p21ras folding which strongly suggests that it is involved in cell proliferation and tumor genesis. To assess the involvement of CCT/TRiC in tumor genesis, we quantified its expression levels and activity in 18 cancer, one non-cancer human cell lines and a non-cancer human liver. We show that the expression levels of CCT/TRiC in cancer cell lines are higher than that in normal cells. However, CCT/TRiC activity does not always correlate with its expression levels. We therefore documented the expression levels of CCT/TRiC modulators and partners PhLP3, Hop/P60, prefoldin and Hsc/Hsp70. Our analysis reveals a functional interplay between molecular chaperones that might account for a precise modulation of CCT/TRiC activity in cell proliferation through changes in the cellular levels of prefoldin and/or Hsc/ p70 and CCT/TRiC client protein availability. Our observation and approaches bring novel insights in the role of CCT/TRiC-mediated protein folding machinery in cancer cell development.
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...vity. Hsc/p70 Modulate CCT/TRiC Activity CCT/TRiC cooperates with other molecular chaperones [2]. Hsc 70 and Hsp70 (Hsc/p70) have been shown to promote client proteins binding to CCT/TRiC for example =-=[34,35]-=-. To determine whether the Hsc/p70 expression levels correlate with that of CCT/TRiC activity, the amounts of Hsc/p70 in the cancer cell line extracts we used throughout this study were quantified by ...

Maximilians-Universität München Chaperonin-Catalyzed Rescue of Kinetically Trapped States in Protein Folding

by Jyoti Sinha, Ehrenwörtliche Versicherung, München Den, Gutacher Dr. F. Ulrich Hartl
"... I am grateful to Dr. Manajit Hayer-Hartl and Prof. Dr. F. Ulrich Hartl for giving me the opportunity to learn and interact with some of the best minds. I would like to take this opportunity to thank them for their encouragement, faith, continual support and giving me the freedom to learn from my mis ..."
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I am grateful to Dr. Manajit Hayer-Hartl and Prof. Dr. F. Ulrich Hartl for giving me the opportunity to learn and interact with some of the best minds. I would like to take this opportunity to thank them for their encouragement, faith, continual support and giving me the freedom to learn from my mistakes. Their ideas and advice have been crucial for development of this project and me as a person. I would like to thank PD. Dr. Konstanze Winklhofer for being a co-referee of my thesis and my thesis advisory committee members Prof. Dr. Dr. Walter Neupert and Prof. Dr. Alexander Buchberger. I would also like to thank our very competent and helpful support system Andrea, Silke and Evelyn who were always there with kind words and solutions to all my administrative and other problems making my stay in Munich smooth. I am also grateful to Elisabeth, Bernd, Dirk, Nadine, and Emmanuel for all their logistical support and help. I am indebted to all my colleagues in the department of cellular biochemistry and specially office A-1 for making the working and learning a pleasurable experience. In particular, help and suggestions provided by Alex Hastie has been valuable to
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...tion by enclosing protein molecules in a nano-compartment, so that folding can occur unimpaired by aggregation. It is interesting to note that the eukaryotic chaperonin interacts directly with Hsp70 (=-=Cuéllar et al., 2008-=-), and thus can be recruited to nascent chains during protein synthesis (McCallum et al., 2000). This functional coupling between different chaperones facilitates co-translational folding and avoids t...

unknown title

by Xue-hai Liang, Wen Shen, Hong Sun, Thazha P. Prakash, Stanley T. Crooke , 2014
"... TCP1 complex proteins interact with phosphorothioate oligonucleotides and can co-localize in oligonucleotide-induced nuclear bodies in mammalian cells ..."
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TCP1 complex proteins interact with phosphorothioate oligonucleotides and can co-localize in oligonucleotide-induced nuclear bodies in mammalian cells
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... ASO/protein complex may be involved in ASO translocation across membranes, which can be facilitated by TCP1 chaperone proteins. In addition, hsc70, a protein that can form a stable complex with TCP1 =-=(39)-=-, is involved in the release of clathrin from clathrin-coated vesicles (40), implying that TCP1 complex may also be able to play a role in ASO release from the endocytosis-related structures. Further ...

unknown title

by Chun Wan, Jeffrey Lai, Chun Wan, Jeffrey Lai, Gregory F. Burton, Allen R. Buskirk, David M. Belnap, Jeffrey Barrow , 2012
"... This Dissertation is brought to you for free and open access by BYU ScholarsArchive. It has been accepted for inclusion in All Theses and Dissertations by an authorized administrator of BYU ScholarsArchive. For more information, please contact scholarsarchive@byu.edu. ..."
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This Dissertation is brought to you for free and open access by BYU ScholarsArchive. It has been accepted for inclusion in All Theses and Dissertations by an authorized administrator of BYU ScholarsArchive. For more information, please contact scholarsarchive@byu.edu.
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...ion is the observation that RGS was recruited to CCT by Gβ5,sleading to the formation of RGS7-Gβ5-CCT ternary complex intermediate [122].sPrevioussevidence has shown that RGS7 can interact with Hsc70 =-=[123, 124]-=-, suggesting that Hsc70 cansdeliver nascent RGS proteins to the Gβ5-CCT complex. After the Gβ5-RGS complex is formed,sit can be released from CCT to interact with membrane anchoring proteins and event...

unknown title

by Xue-hai Liang, Wen Shen, Hong Sun, Thazha P. Prakash, Stanley T. Crooke , 2014
"... TCP1 complex proteins interact with phosphorothioate oligonucleotides and can co-localize in oligonucleotide-induced nuclear bodies in mammalian cells ..."
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TCP1 complex proteins interact with phosphorothioate oligonucleotides and can co-localize in oligonucleotide-induced nuclear bodies in mammalian cells
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... ASO/protein complex may be involved in ASO translocation across membranes, which can be facilitated by TCP1 chaperone proteins. In addition, hsc70, a protein that can form a stable complex with TCP1 =-=(39)-=-, is involved in the release of clathrin from clathrin-coated vesicles (40), implying that TCP1 complex may also be able to play a role in ASO release from the endocytosis-related structures. Further ...

unknown title

by Xue-hai Liang, Wen Shen, Hong Sun, Thazha P. Prakash, Stanley T. Crooke , 2014
"... TCP1 complex proteins interact with phosphorothioate oligonucleotides and can co-localize in oligonucleotide-induced nuclear bodies in mammalian cells ..."
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TCP1 complex proteins interact with phosphorothioate oligonucleotides and can co-localize in oligonucleotide-induced nuclear bodies in mammalian cells
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... ASO/protein complex may be involved in ASO translocation across membranes, which can be facilitated by TCP1 chaperone proteins. In addition, hsc70, a protein that can form a stable complex with TCP1 =-=(39)-=-, is involved in the release of clathrin from clathrin-coated vesicles (40), implying that TCP1 complex may also be able to play a role in ASO release from the endocytosis-related structures. Further ...

der Ludwig-Maximilians-Universität München The Eukaryotic Chaperonin TRiC Domain-Wise Folding of Multi-Domain Proteins

by Florian Rüßmann, Herrn Prof Dr, F. Ulrich Hartl, Eidesstattliche Versicherung, Florian Rüßmann
"... I would like to thank Prof. Dr. F.-Ulrich Hartl for giving me the opportunity to work in his laboratory and for his optimism and his creative input during the entire course of my project. I would like to thank my supervisors Dr. Stephanie Etchells and Dr. Andreas Bracher. Many obstacles have been ov ..."
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I would like to thank Prof. Dr. F.-Ulrich Hartl for giving me the opportunity to work in his laboratory and for his optimism and his creative input during the entire course of my project. I would like to thank my supervisors Dr. Stephanie Etchells and Dr. Andreas Bracher. Many obstacles have been overcome by their support. Their questions and ideas shaped the project significantly. I would like to thank Dr. Markus Stemp who had started the project and who introduced me into many of the necessary skills and techniques. I would like to thank my colleagues in the lab for creating a unique working atmosphere and for many shared moments that I will never forget. I would like to thank Dr. Birgitta Beatrix and Prof. Dr. Don Lamb for the discussions during the TAC meetings that provided helpful external input. I would like to thank the members of my PhD committee PD Dr. Dr. Konstanze Winklhofer, PD
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...t al., 1998). However, a cryo-EM structure of the nucleotide-binding domain of Hsc70 in complex with TRiC suggests that transfer might be enabled also by a direct interaction between Hsp70s and TRiC (=-=Cuellar et al., 2008-=-). - 13 -2.3 Different Classes of Molecular Chaperones The different classes of molecular chaperones are very diverse with regard to their structure. Hsp60s, Hsp70s and Hsp90s undergo ATP-dependent c...

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