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The Arl3 and Arl1 GTPases co‐operate with Cog8 to regulate selective autophagy via Atg9 trafficking
Author(s) -
Wang IHao,
Chen YiJie,
Hsu JiaWei,
Lee Fang Jen
Publication year - 2017
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12498
Subject(s) - golgi apparatus , endosome , microbiology and biotechnology , biology , autophagy , small gtpase , gtpase , vacuole , rab , cytoplasm , transport protein , vesicular transport proteins , retromer , signal transduction , biochemistry , endoplasmic reticulum , vacuolar protein sorting , apoptosis , intracellular
The Arl3‐Arl1 GTPase cascade plays important roles in vesicle trafficking at the late Golgi and endosomes. Subunits of the conserved oligomeric Golgi ( COG ) complex, a tethering factor, are important for endosome‐to‐Golgi transport and contribute to the efficient functioning of the cytoplasm‐to‐vacuole targeting (Cvt) pathway, a well‐known selective autophagy pathway. According to our findings, the Arl3‐Arl1 GTPase cascade co‐operates with Cog8 to regulate the Cvt pathway via Atg9 trafficking. arl3cog8Δ and arl1cog8Δ exhibit profound defects in aminopeptidase I maturation in rich medium. In addition, the Arl3‐Arl1 cascade acts on the Cvt pathway via dynamic nucleotide binding. Furthermore, Atg9 accumulates at the late Golgi in arl3cog8Δ and arl1cog8Δ cells under normal growth conditions but not under starvation conditions. Thus, our results offer insight into the requirement for multiple components in the Golgi‐endosome system to determine Atg9 trafficking at the Golgi, thereby regulating selective autophagy.