{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTCP1 is an essential subunit of the cytosolic chaperonin complex TRiC (also known as CCT) that plays a critical role in the ATP‐dependent folding of newly synthesized proteins. It has been shown to promote the maturation of key cytoskeletal proteins—most notably tubulin and actin—thereby ensuring the formation of α–β tubulin heterodimers and proper assembly of the microtubule network. TCP1‐containing complexes not only assist in folding nascent tubulin into an assembly‐competent and protease‐resistant conformation but also participate in microtubule‐mediated processes such as spindle formation during cell division. In addition, TCP1 and its associated subunits have been implicated in preventing aberrant protein aggregation, including that of amyloidogenic species, thereby contributing to cellular proteostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAlterations in TCP1 expression or function have been increasingly linked to a variety of human diseases. In several cancers—including breast, hepatocellular, ovarian and neuroendocrine tumors—TCP1 and other TRiC subunits are frequently overexpressed or genetically altered, where they support the folding and stability of oncogenic proteins (for example, the AML1–ETO fusion oncoprotein) and thereby influence cell proliferation, survival and disease outcome. Moreover, aberrant TCP1 levels have been associated with neurodegenerative and developmental disorders, highlighting its potential as both a biomarker and a therapeutic target. These findings indicate that dysregulation of cytoskeletal proteostasis, mediated in part by TCP1, may contribute significantly to pathogenesis and tumor progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its chaperone function in protein folding, the TCP1 gene is notable for its deep evolutionary conservation and unique genomic organization. Mapped to human chromosome 6—and found in diverse species from yeast to Tetrahymena—the TCP1 locus is part of a complex genomic landscape that sometimes involves overlapping gene structures. Detailed structural and mass spectrometry analyses have revealed that TCP1, along with its partner subunits, undergoes specific N‐terminal processing events that promote proper assembly into the hetero-oligomeric ring complex. Moreover, TCP1 has been found to interact directly with other cellular factors such as LOX‐1 and HtrA3, expanding its functional network and suggesting additional roles in cellular signaling and stress responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "22", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "M B Yaffe, G W Farr, D Miklos, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Two members of the TRiC chaperonin complex, CCT2 and TCP1 are essential for survival of breast cancer cells and are linked to driving oncogenes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Cell Res (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexcr.2015.02.005"}], "href": "https://doi.org/10.1016/j.yexcr.2015.02.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25704758"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25704758"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Xudong Jiang, Wenjuan Mao, Ziyi Yang, et al. 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