Autophagy initiation by ULK complex assembly on ER tubulovesicular regions marked by ATG9 vesicles

Karanasios, Eleftherios; Walker, Simon; Okkenhaug, Hanneke; Manifava, Maria; Hummel, Eric; Zimmermann, H.; Ahmed, Qashif; Domart, Marie-Charlotte; Collinson, Lucy M.; Ktistakis, Nicholas T.

doi:10.1038/ncomms12420

Cited by 272 publications

(272 citation statements)

References 68 publications

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“…In mammalian cells, approximately 54% of the LC3 puncta colocalize with the ERES protein Sec16 (Graef et al, 2013), a scaffold protein that interacts with multiple COPII coat subunits to regulate coat assembly (Budnik and Stephens, 2009). Similar observations were also made by others (Karanasios et al, 2016). Additionally, loss of function temperature-sensitive mutations in genes that encode secretory machinery such as SEC16 or SEC12 , the guanine nucleotide exchange factor (GEF) for Sar1 (Barlowe and Schekman, 1993), inhibit autophagosome formation (Graef et al, 2013; Ishihara et al, 2001).…”

Section: Early Secretory Pathwaysupporting

confidence: 92%

Crosstalk between the Secretory and Autophagy Pathways Regulates Autophagosome Formation

2017

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The induction of autophagy by nutrient deprivation leads to a rapid increase in the formation of autophagosomes, unique organelles that replenish the cellular pool of nutrients by sequestering cytoplasmic material for degradation. The urgent need for membrane to form autophagosomes during starvation, to maintain homeostasis, leads to a dramatic rearrangement of intracellular membranes. Here we discuss recent findings that have begun to uncover how different parts of the secretory pathway directly and indirectly contribute to autophagosome formation during starvation.

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Section: Early Secretory Pathwaysupporting

confidence: 92%

Crosstalk between the Secretory and Autophagy Pathways Regulates Autophagosome Formation

2017

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“…In mammalian cells, nucleation of autophagosomes occurs in the vicinity of the ER and the Atg9 compartment (Karanasios et al, 2016). Interestingly, membrane fractionation identified the ER-Golgi intermediate compartment (ERGIC), which resides adjacent to the ER, as the site of lipidation of the Atg8 homologue LC3 (Ge et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Sec24 phosphorylation regulates autophagosome abundance during nutrient deprivation

Davis

Wang

Zhu

et al. 2016

eLife

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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 Saccharomyces cerevisiae 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.DOI: http://dx.doi.org/10.7554/eLife.21167.001

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“…In support of the former, treating mammalian cells with the ER-export inhibitor FLI-06 (Krämer et al. , 2013) reduces the number of autophagosomes under starvation conditions (Karanasios et al. , 2016).…”

Section: Multitasking Proteins In Secretion and Autophagymentioning

confidence: 99%

The link between autophagy and secretion: a story of multitasking proteins

Farhan

Kundu

Ferro‐Novick

2017

MBoC

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The secretory and autophagy pathways can be thought of as the biosynthetic (i.e., anabolic) and degradative (i.e., catabolic) branches of the endomembrane system. In analogy to anabolic and catabolic pathways in metabolism, there is mounting evidence that the secretory and autophagy pathways are intimately linked and that certain regulatory elements are shared between them. Here we highlight the parallels and points of intersection between these two evolutionarily highly conserved and fundamental endomembrane systems. The intersection of these pathways may play an important role in remodeling membranes during cellular stress.

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Autophagy initiation by ULK complex assembly on ER tubulovesicular regions marked by ATG9 vesicles

Cited by 272 publications

References 68 publications

Crosstalk between the Secretory and Autophagy Pathways Regulates Autophagosome Formation

Crosstalk between the Secretory and Autophagy Pathways Regulates Autophagosome Formation

Sec24 phosphorylation regulates autophagosome abundance during nutrient deprivation

The link between autophagy and secretion: a story of multitasking proteins

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