Sec24 phosphorylation regulates autophagosome abundance during nutrient deprivation

Endoplasmic Reticulum (ER)-derived COPII coated vesicles constitutively transport secretory cargo to the Golgi. However, during starvation-induced stress, COPII vesicles have been implicated as a membrane source for autophagosomes, distinct organelles that engulf cellular components for degradation...

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Bibliographic Details
Published in:eLife 2016-11, Vol.5
Main Authors: Davis, Saralin, Wang, Juan, Zhu, Ming, Stahmer, Kyle, Lakshminarayan, Ramya, Ghassemian, Majid, Jiang, Yu, Miller, Elizabeth A, Ferro-Novick, Susan
Format: Article
Language:English
Subjects:
Autophagosomes - metabolism
Autophagy
Autophagy-Related Proteins - metabolism
Biodegradation
C-Terminus
Casein
Casein kinase I
Casein Kinase I - metabolism
Cell Biology
Coated vesicles
COPII vesicles
Endoplasmic reticulum
Golgi apparatus
Hrr25
Kinases
Mass spectrometry
Membrane Proteins - metabolism
Mutation
Observations
Organelle Biogenesis
Organelles
Phagocytosis
Phagosomes
Phosphorylation
Physiological aspects
Protein Binding
Protein Processing, Post-Translational
Proteins
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins - metabolism
Scientific imaging
Secretory pathway
Secretory vesicles
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Summary:Endoplasmic Reticulum (ER)-derived COPII coated vesicles constitutively transport secretory cargo to the Golgi. However, during starvation-induced stress, COPII vesicles have been implicated as a membrane source for autophagosomes, distinct organelles that engulf cellular components for degradation by macroautophagy (hereafter called autophagy). How cells regulate core trafficking machinery to fulfill dramatically different cellular roles in response to environmental cues is unknown. Here we show that phosphorylation of conserved amino acids on the membrane-distal surface of the COPII cargo adaptor, Sec24, reprograms COPII vesicles for autophagy. We also show casein kinase 1 (Hrr25) is a key kinase that phosphorylates this regulatory surface. During autophagy, Sec24 phosphorylation regulates autophagosome number and its interaction with the C-terminus of Atg9, a component of the autophagy machinery required for autophagosome initiation. We propose that the acute need to produce autophagosomes during starvation drives the interaction of Sec24 with Atg9 to increase autophagosome abundance.
ISSN:2050-084X
2050-084X
DOI:10.7554/elife.21167