Intracellular β-Tubulin/Chaperonin Containing TCP1-β Complex Serves as a Novel Chemotherapeutic Target against Drug-Resistant Tumors

Abstract

In the present study, treatment of HEK-293 cells with the synthetic small molecule N-iodoacetyl-tryptophan

Tyrosine-dependent capture of CAP-Gly domain‐containing proteins in complex mixture by EB1 C-terminal peptidic probes

“…This is consistent with the recently published structure of CCT in complex with tubulin combined with crosslinking/MS analysis that suggests a direct interaction between the C-terminal domains of α-or β-tubulin and CCT2 [32]. This is also consistent with studies suggesting that the tubulin-CCT interaction is initiated by the C-terminal domain of tubulin [33,34]. A proteomic study on tubulin-binding proteins in plant cells identified CCT7 (TCP-1 η subunit) [35].…”

Proteomic Analysis of Frankliniella occidentalis and Differentially Expressed Proteins in Response toTomato Spotted Wilt VirusInfection

“…Both alpha-and beta-tubulin were identified in the L1 proteome, and various tubulin proteins have been shown to play a role in phagocytosis (31,41) and in regulation of apoptosis (42). A protein spot that matched lethal giant larvae homologue was found, and one possible function for this protein is the induction of salivary gland cell autophagic cell death.…”

Overexpression of CCT8 and its significance for tumor cell proliferation, migration and invasion in glioma

“…Reduction of the CCT or CCT subunit could result in growth arrest, with significant alterations in cell morphology and motility [14]. Moreover, the CCT proteins promote the development of several tumor types, including breast cancer [4], colorectal cancer [7,24,27,28], uterine sarcoma [21], lung carcinoma [8,24], ovarian cancer [22], and multitudinous tumor cells [1,25]. Recent studies have suggested that CCT8 might be upregulated in colon, breast and hepatocellular carcinoma specimens [17,35,36].…”