2022年4月14日 · CCT2 associates with aggregation-prone proteins independent of cargo ubiquitination and interacts with autophagosome marker ATG8s through a non-classical VLIR motif. In addition, CCT2 regulates aggrephagy independently of the ubiquitin-binding receptors (P62, NBR1, and TAX1BP1) or chaperone-mediated autophagy.

2022年4月2日 · CCT2是分子伴侣Chaperonin复合体的一个亚基，与复合体一起作为分子伴侣帮助错误折叠的蛋白正确地折叠。 研究发现，CCT2是以单体形式介导聚集体自噬的，因为只有单体形式的CCT2能够暴露出与LC3的结合位点VLIR 结构域。

2025年3月30日 · CCT2 (Chaperonin Containing TCP1 Subunit 2) is a Protein Coding gene. Diseases associated with CCT2 include Aniridia 1 and Leber Plus Disease. Among its related pathways are Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding and Chaperonin-mediated protein folding.

2016年12月8日 · Knockdowns of CCT complex subunits (CCT2/5/7) increased the number and size of autophagosomes/non-acidified lysosomes (yellow vesicles/GFP dots), while the number of acidic autolysosomes (red...

2022年4月5日 · In particular, CCT2 — a subunit of the chaperonin TRiC complex — was implicated in aggregate removal by autophagy both in vitro and in mouse brain. Like ubiquitin-binding aggrephagy receptors,...

2022年4月1日，清华大学生命学院葛亮课题组在 Cell 期刊在线发表题为：CCT2 is an aggrephagy receptor for clearance of solid protein aggregates的研究论文。该研究发现了一种新型的聚集体自噬受体CCT2在清除固态蛋白聚集体中的重要作用。

CCT2, traditionally viewed as a molecular chaperone, has emerged as a novel autophagy receptor that specifically targets solid protein aggregates for degradation. This ubiquitination-independent mode of recognition by CCT2 expands our …

2022年4月1日 · 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.

A recent study from Ge lab reported the TRiC subunit CCT2 (chaperonin containing TCP1 subunit 2) as the first identified specific aggrephagy receptor in mammals. The switch of CCT2's role from a chaperonin to a specific aggrephagy receptor is achieved by CCT2 monomer formation.

T-complex protein 1 subunit beta is a protein that in humans is encoded by the CCT2 gene. [5][6] This gene encodes a molecular chaperone that is member of the TRiC complex. This complex consists of two identical stacked rings, each containing eight different proteins.