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Autophagy regulates the early secretory pathway through interaction between ULK1 and Sec23
Author(s) -
ZHAO Shan,
Gan Wenjia,
Chan Hsaio Chang,
YU Sidney
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.864.16
Subject(s) - autophagy , ulk1 , microbiology and biotechnology , intracellular , secretory pathway , protein kinase a , kinase , autophagy related protein 13 , secretion , biology , chemistry , biochemistry , protein phosphorylation , ampk , endoplasmic reticulum , apoptosis , golgi apparatus
Autophagy is an autodigestive process that maintains the intracellular homeostasis under starvation. Although it has been intensely studied, how it affects the early secretory pathway has not been well characterized. In this study, we found that autophagy changes the morphology of ER exit sites and causes delay in the export of transport cargo proteins from ER exit sites. The serine/threonine kinase ULK1 is a kinase regulating the activation of autophagy. We found that the morphological and functional changes of ER exit sites are mediated by the phosphorylation of Sec23 by ULK1. This event weakens the interaction between Sec23 and Sec31 but strengthens the binding of Sec23 to Sar1. These results uncover connection between the autophagic pathway and the exocytic pathway such that ULK1 decreases traffic of protein vesicles at the stage of ER exit and such regulation helps save energy for the cells when they are under starvation condition. Support or Funding Information This project was supported by Research Grant Council (RGC 14118914)