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Chiu, Shao‐Chih; Huang, Yun‐Ru Jaoying; Wei, Tong‐You Wade; Chen, Jo‐Mei Maureen; Kuo, Yi‐Chun; Huang, Yu‐Ting Jenny; Liao, Yu‐Ting Amber; Yu, Chang‐Tze Ricky
Journal of cellular physiology, January 2022, 2022-01-00, 20220101, Letnik: 237, Številka: 1Journal Article
The Golgi apparatus (GA) translocates to the cell leading end during directional migration, thereby determining cell polarity and transporting essential factors to the migration apparatus. The study provides mechanistic insights into how GA repositioning (GR) is regulated. We show that the methyltransferase PRMT5 methylates the microtubule regulator HURP at R122. The HURP methylation mimicking mutant 122F impairs GR and cell migration. Mechanistic studies revealed that HURP 122F or endogenous methylated HURP, that is, HURP m122, interacts with acetyl‐tubulin. Overexpression of HURP 122F stabilizes the bundling pattern of acetyl‐tubulin by decreasing the sensitivity of the latter to a microtubule disrupting agent nocodazole. HURP 122F also rigidifies GA via desensitizing the organelle to several GA disrupting chemicals. Similarly, the acetyl‐tubulin mimicking mutant 40Q or tubulin acetyltransferase αTAT1 can rigidify GA, impair GR, and retard cell migration. Reversal of HURP 122F‐induced GA rigidification, by knocking down GA assembly factors such as GRASP65 or GM130, attenuates 122F‐triggered GR and cell migration. Remarkably, PRMT5 is found downregulated and the level of HURP m122 is decreased during the early hours of wound healing‐based cell migration, collectively implying that the PRMT5‐HURP‐acetyl‐tubulin axis plays the role of brake, preventing GR and cell migration before cells reach empty space.
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