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Flashlight into the function of unannotated C11orf52 with global and glyco- pretomic analysis
Yeji Yang,Heeyoun Hwang,Ji Eun Im,Kyungha Lee,Seong Hee Bhoo,Jong Shin Yoo,Yun-Hee Kim,Jin Young Kim 한국당과학회 2022 한국당과학회 학술대회 Vol.2022 No.07
For an enhanced understanding of the biological mechanisms of human disease, it is essential to investigate protein functions. In a previous study, we developed a prediction method of gene ontology (GO) terms by the I-TASSER/COFACTOR result, and we applied this to uPE1 in chromosome 11. Furthermore, to validate the bioinformatics prediction of C11orf52, we utilized affinity purification and mass spectrometry to identify interacting partners of C11orf52. Using immunoprecipitation methods with three different peptide tags (Myc, Flag, and 2B8) in HEK 293T cell lines, we identified 79 candidate proteins that are expected to interact with C11orf52. The results of a pathway analysis of the GO and STRING database with candidate proteins showed that C11orf52 could be related to signaling receptor binding, cell−cell adhesion, and ribosome biogenesis. Then, we selected three partner candidates of DSG1, JUP, and PTPN11 for verification of the interaction with C11orf52 and confirmed them by colocalization at the cell−cell junctions by coimmunofluorescence experiments. In fact, cell-cell interactions and cell adhesion could be affected by glycosylation of adhesive molecules. Here, we focused on changes in protein expressions and glycosylation patterns caused by overexpression of C11orf52. Differentially expressed proetins and glycosylations were identified with TMT-based quantitative global and glyco- pretomic analysis and it will help to clarify how C11orf52 works in cells.