The TRiC/CCT Chaperonin and Its Role in Uncontrolled Proliferation
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The TRiC/CCT Chaperonin and Its Role in Uncontrolled Proliferation. / Wang, Dan Yang; Kamuda, Kamila; Montoya, Guillermo; Mesa, Pablo.
HSF1 and Molecular Chaperones in Biology and Cancer. ed. / Marc Laurence Mendillo; David Pincus; Ruth ScherzShouval. Springer, 2020. p. 21-40 (Advances in Experimental Medicine and Biology, Vol. 1243).Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
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TY - CHAP
T1 - The TRiC/CCT Chaperonin and Its Role in Uncontrolled Proliferation
AU - Wang, Dan Yang
AU - Kamuda, Kamila
AU - Montoya, Guillermo
AU - Mesa, Pablo
PY - 2020
Y1 - 2020
N2 - The cell cycle is a sophisticated space-time regulated mechanism where a wide variety of protein modules and complexes associate functioning in a concerted manner to regulate and transfer the genetic material to daughter cells. CCT (chaperonin containing TCP-1, also known as TRiC) is a molecular machine that forms a high molecular weight complex (1000 KDa). CCT is emerging as a key molecule during mitosis due to its essential role in the folding of many important proteins involved in cell division (Cdh1, Plk1, p27, Cdc20, PP2a regulatory subunits, tubulin or actin) suggesting its involvement in uncontrolled proliferation. The assembly is formed by eight different subunits called CCT alpha, beta, gamma, delta, epsilon, zeta, eta and theta in mammals corresponding to CCT1-8 in yeast. CCT/TRiC is organized in a unique intra- and inter-ring arrangement. The chaperonin monomers share a common domain structure including an equatorial domain, which contains all the inter-ring contacts, most of the intra-ring contacts and the ATP binding site, whose binding and hydrolysis triggers the conformational changes that take place during the functional cycle. All chaperonins display an open substrate-receptive conformation, where the unfolded protein is recognized and trapped, and a closed conformation where the substrate is isolated from the bulk of the intracellular environment. In this chapter we discuss the complex set of intra- and inter-ring allosteric signals during chaperonin function.
AB - The cell cycle is a sophisticated space-time regulated mechanism where a wide variety of protein modules and complexes associate functioning in a concerted manner to regulate and transfer the genetic material to daughter cells. CCT (chaperonin containing TCP-1, also known as TRiC) is a molecular machine that forms a high molecular weight complex (1000 KDa). CCT is emerging as a key molecule during mitosis due to its essential role in the folding of many important proteins involved in cell division (Cdh1, Plk1, p27, Cdc20, PP2a regulatory subunits, tubulin or actin) suggesting its involvement in uncontrolled proliferation. The assembly is formed by eight different subunits called CCT alpha, beta, gamma, delta, epsilon, zeta, eta and theta in mammals corresponding to CCT1-8 in yeast. CCT/TRiC is organized in a unique intra- and inter-ring arrangement. The chaperonin monomers share a common domain structure including an equatorial domain, which contains all the inter-ring contacts, most of the intra-ring contacts and the ATP binding site, whose binding and hydrolysis triggers the conformational changes that take place during the functional cycle. All chaperonins display an open substrate-receptive conformation, where the unfolded protein is recognized and trapped, and a closed conformation where the substrate is isolated from the bulk of the intracellular environment. In this chapter we discuss the complex set of intra- and inter-ring allosteric signals during chaperonin function.
KW - Chaperonines
KW - Molecular machines
KW - Cell cycle
KW - Protein folding
KW - Allosterism
KW - ATP hydrolysis
KW - Protein-protein interaction
KW - X-ray
KW - cryoEM
KW - ANAPHASE-PROMOTING COMPLEX
KW - EUKARYOTIC CHAPERONIN
KW - MOLECULAR CHAPERONE
KW - CYTOPLASMIC CHAPERONIN
KW - CYTOSOLIC CHAPERONIN
KW - CCT CHAPERONIN
KW - SACCHAROMYCES-CEREVISIAE
KW - CONFORMATIONAL-CHANGES
KW - CRYSTAL-STRUCTURE
KW - LID CLOSURE
U2 - 10.1007/978-3-030-40204-4_2
DO - 10.1007/978-3-030-40204-4_2
M3 - Book chapter
C2 - 32297209
SN - 978-3-030-40203-7
T3 - Advances in Experimental Medicine and Biology
SP - 21
EP - 40
BT - HSF1 and Molecular Chaperones in Biology and Cancer
A2 - Mendillo, Marc Laurence
A2 - Pincus, David
A2 - ScherzShouval, Ruth
PB - Springer
ER -
ID: 249860706