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Glycosylation affects the stability and subcellular distribution of human PAT 1 protein
Author(s) -
Luo Hongjie,
Zhao Lingling,
Ji Xin,
Zhang Xiangxiang,
Jin Yaping,
Liu Wei
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12567
Subject(s) - endoplasmic reticulum , hek 293 cells , lysosome , glycosylation , microbiology and biotechnology , mtorc1 , endoplasmic reticulum associated protein degradation , chemistry , glycoprotein , biochemistry , biology , unfolded protein response , phosphorylation , receptor , enzyme , protein kinase b
The amino acid transporter PAT 1 is typically expressed on the lysosome and plasma membranes in various human tissues. Glycosylation has been shown to be critical for the cell surface expression of PAT 1, but not for its stability, in Xenopus oocytes. Here, we report that the glycosylation‐deficient mutant of PAT 1 ( PAT 1 3 NQ ) is unstable and is degraded mainly via the endoplasmic reticulum‐associated degradation pathway in HEK 293 cells. Interestingly, PAT 1 3 NQ binds preferentially to the plasma membrane rather than to the lysosome. Consistent with this altered distribution, overexpression of PAT 1 3 NQ fails to inhibit the mechanistic target of rapamycin complex 1 ( mTORC 1). Our data suggest that glycosylation affects the stability and localization of PAT 1 in HEK 293 cells and the subcellular distribution of PAT 1 is a factor affecting mTORC 1 activity.