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Cct2 chaperonin

WebApr 14, 2024 · Here, we identify the chaperonin subunit CCT2 as an autophagy receptor regulating the clearance of aggregation-prone proteins in the cell and the mouse brain. CCT2 associates with aggregation-prone proteins independent of cargo ubiquitination and interacts with autophagosome marker ATG8s through a non-classical VLIR motif. WebApr 22, 2014 · The primary cytosolic eukaryotic chaperonin is the tailless complex protein-1 (TCP-1) ring complex (commonly abbreviated TRiC, and also known as complex containing TCP-1 or CCT). TRiC is a large complex (1 MDa) composed of eight homologous but distinct subunits (CCT 1–8), arranged in two stacked octameric rings to form two interior …

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• Kubota H, Hynes G, Carne A, Ashworth A, Willison K (Feb 1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Current Biology. 4 (2): 89–99. doi:10.1016/S0960-9822(94)00024-2. PMID 7953530. S2CID 31300131. • Llorca O, Smyth MG, Carrascosa JL, Willison KR, Radermacher M, Steinbacher S, Valpuesta JM (Jul 1999). "3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding confor… WebApr 4, 2024 · Manipulating CCT2 levels in individual breast, neuroblastoma, and prostate cancer cells revealed the strategic importance of this chaperonin subunit in supporting the metastatic cancer phenotype. ttc driver assaulted https://combustiondesignsinc.com

10576 - Gene ResultCCT2 chaperonin containing TCP1 subunit 2 [ (human)]

WebApr 1, 2024 · Protein aggregation is a hallmark of multiple human pathologies. Autophagy selectively degrades protein aggregates via aggrephagy. How selectivity is achieved has been elusive. Here, we … WebABOUT - Payne Township WebAug 21, 2024 · Chaperonin‐containing TCP‐1 subunit 2 (CCT2)’s dual function in preventing protein aggregation and removing protein aggregates. CCT2 can function as a component of the TRiC complex to suppress protein misfolding and aggregation; also, it can act as a monomeric autophagy receptor to facilitate the clearance of solid protein … phoebe\\u0027s holiday hoggery

Native mass spectrometry analyses of chaperonin complex …

Category:TRiC/CCT Chaperonin: Structure and Function SpringerLink

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Cct2 chaperonin

The CCT chaperonin is a novel regulator of Ca2+ signaling …

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Cct2 chaperonin

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WebIn other projects. CCT2 (gen) - CCT2 (gene) CCT2; Identifikátory; Aliasy: CCT2, 99D8.1, CCT-beta, CCTB, HEL-S-100n, PRO1633, TCP-1-beta, chaperonin obsahující ... WebChaperonin containing tailless complex polypeptide 1 (CCT) or tailless complex polypeptide 1 ring complex (TRiC) is an essential eukaryotic molecular chaperone. It is a multi-subunit oligomer of two rings of eight individual protein subunits. When assembled, each of the eight CCT subunits occupies a specific position within each chaperonin ring. Thus a …

WebJan 21, 2024 · Chaperonin-containing TCP-1 (CCT or TRiC) is a multi-subunit complex that folds many of the proteins essential for cancer development. CCT is expressed in diverse cancers and could be an ideal ... WebSep 30, 1997 · The well-studied chaperonin, GroEL, in Escherichia coli is a double toroid multimeric ATPase protein complex with seven identical subunits in each ring. In contrast, eight different but closely related subunits, Cct1p–Cct8p, have been identified in the eukaryotic chaperonin complex, Cct. ... cct2–1 (bin3–1) (MATa ura3–52 his4–539 lys2 ...

WebApr 30, 2024 · CCT, a type II chaperonin, is a multi-subunit protein-folding complex that interacts with many oncoproteins and mutant tumor suppressors. CCT subunits are …

WebJan 1, 2024 · including CCT2-CCT4, CCT1-CCT3, CCT6-CCT8, and CCT7-CCT5; and there exists a two fold axis between its two rings, resulting in two homotypic subunit interactions across the rings (Cong et al. 2010 ... ttc driver wageWebOct 24, 2016 · This chaperonin is also essential for the folding of many proteins involved in oncogenesis, such as p53, VHL tumor suppressor, and STAT3 (refs. ... CCT2, CCT4, and CCT5) bind ATP at its ... ttc drive inWebFeb 5, 2024 · Orthologous to human CCT2 (chaperonin containing TCP1 subunit 2). [provided by Alliance of Genome Resources, Apr 2024] Other designations. T-complex protein 1 subunit beta, CCT-beta, TCP-1-beta, chaperonin subunit 2 (beta) GeneRIFs: Gene References Into Functions. CCT2 is an aggrephagy receptor for clearance of solid … phoebe\u0027s holiday song sweaterWebSep 15, 2024 · Such data suggest that CCT2 may have a unique and essential activity in the chaperonin complex. CCT2 is postulated to be the first subunit to load onto a CCT5 homo-oligomer “template” that initiates assembly of the CCT complex , has a long half-life (~8 hrs) , and has one of the highest affinities for ATP . phoebe\\u0027s holiday song sweaterWebJun 22, 2024 · The eukaryotic chaperonin TRiC/CCT is a large ATP-dependent complex essential for cellular protein folding. Its subunit arrangement into two stacked eight-membered hetero-oligomeric rings is ... phoebe\\u0027s home bryanWebchaperonin has a build-in lid in the apical domain that can shut close the chamber (Fig. 19.2a–c). The archaea group II chaperonin has eight or nine subunits per ring, phoebe\u0027s home bryanWebFeb 5, 2024 · Orthologous to human CCT2 (chaperonin containing TCP1 subunit 2). [provided by Alliance of Genome Resources, Apr 2024] Other designations. T-complex … ttcdw 脚本