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Results for “TRAPPC2L”

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PubMed2025

Proteomic hub proteins CDKN2B, TRAPPC2L, WFS1, and ARPP19 drive biochemical recurrence and metastatic progression in prostate cancer: Protein macromolecule action.

The biological characteristics and metastasis mechanism of prostate cancer are complex, involving the important role of many proteins in cell transcriptional regulation. This study focused on the role of the proteomic hub proteins CDKN2B, TRAPPC2L, WFS1 and ARPP19 in the biochemical recurrence and metastasis progression of prostate cancer. Cross-platform transcriptome integration and differential expression analysis were used to evaluate transcriptome characteristics in a prostate cancer cohort. Functional enrichment analysis was performed by gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway annotation, and weighted gene co-expression network analysis (WGCNA) was used to investigate cancer progression subtypes. It was found that prostate cancer progression showed significant transcriptome heterogeneity, and low-expression genes dominated. We reveal the important role of epithelial-immune interactions and inflammatory signaling in transcriptional remodeling in prostate cancer. The co-expression network topology analysis showed that the immune-metabolic center module plays a central role in cancer progression. CDKN2B was identified as a key transcriptional determinant in prostate cancer typing, while TRAPPC2L and WFS1 acted as core transcriptional regulators, driving metastatic heterogeneity. ARPP19 and LOC650152 also show important transcriptional driving effects in advanced prostate cancer.

Humans↗
PubMed2026

A subcomplex comprising TRAPPC11, TRAPPC12, TRAPPC13 and the fungal TRAPPC2L homolog, Tca17, directs TRAPPIII to autophagy.

Transport protein particle complexes (TRAPPs) are master regulators of membrane trafficking. TRAPPs are targeted to different locales by pathway-specific subunits decorating a core hetero-heptamer to build TRAPPII (Golgi exit) and TRAPPIII (autophagosomes and ER-Golgi trafficking). Metazoan and Arabidopsis TRAPPIII have three components, TRAPPC11, TRAPPC12 and TRAPPC13 (hereafter denoted TRAPPC11/12/13), that are absent from budding yeast. We studied TRAPPC11/12/13 in the related ascomycete Aspergillus nidulans, where TRAPPC11 and TRAPPC12 localize to pre-autophagosomes and their ablation impairs autophagy. We found that two stable subcomplexes containing Tca17, the homolog of metazoan TRAPPC2L, coexist - one includes the TRAPPII-specific subunits Trs120, Trs130 and Trs65 whereas the other contains the TRAPPIII-specific subunits TRAPPC11/12/13. Both are recruited to core TRAPP by Tca17, which therefore plays a crucial role by determining the physiological role of TRAPP. TRAPPIII also exists in two versions, TRAPPIIIa and TRAPPIIIb, both of which contain Trs85, the homolog of metazoan TRAPPC8, but with only TRAPPIIIb containing TRAPPC11/12/13, which target TRAPPIII to autophagy. This study might help characterize potentially pathogenic mutations affecting human TRAPPC11/12/13, facilitating assessment of their functional consequences in a genetically amenable ascomycete.

Autophagy↗