Yanwen Chen, Ruijie Liu, Shaoxing Zhang, Yuxin Zhang, Qiange Lin, Yilin Ye, Shuying Yuan, Xinrong Lu, Linfei Wang, Li Chen, Guiqin Sun
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引用次数: 0
Abstract
N-glycanase 1 (NGLY1) is involved in intracellular misfolded protein degradation, releasing a de-N-glycosylated protein and a complete N-oligosaccharide. Enzymatic defects in NGLY1 may cause NGLY1-related congenital disorder of deglycosylation (NGLY1-CDDG). NGLY1 patients exhibit cognition and coordination defects, and the regulatory impact of NGLY1 in the organism deserves in-depth investigation. In this study, we established NGLY1-knockdown human foreskin fibroblasts-1 (HFF-1) cells and observed mitochondrial function impairments. We conservatively suggest that NGLY1 has global regulatory roles within cells. The Calnexin/IP3R/VDAC1 axis acts as a communication bridge and represents one mechanism underlying NGLY1-mediated modulation of mitochondrial function. This has significant implications for addressing the clinical disease problems presented by NGLY1-CDDG.
期刊介绍：
The Journal of Cellular Biochemistry publishes descriptions of original research in which complex cellular, pathogenic, clinical, or animal model systems are studied by biochemical, molecular, genetic, epigenetic or quantitative ultrastructural approaches. Submission of papers reporting genomic, proteomic, bioinformatics and systems biology approaches to identify and characterize parameters of biological control in a cellular context are encouraged. The areas covered include, but are not restricted to, conditions, agents, regulatory networks, or differentiation states that influence structure, cell cycle & growth control, structure-function relationships.
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