Entry and Exit Mechanisms at the cis-Face of the Golgi Complex

Lorente-Rodríguez, Andrés; Barlowe, Charles

doi:10.1101/cshperspect.a005207

Cited by 37 publications

(31 citation statements)

References 109 publications

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“…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). During starvation, the ERES were found to translocate to the ERGIC fraction, and although the ERGIC is typically a location of COPI vesicle budding (Lorente-Rodríguez and Barlowe, 2011), COPII vesicle budding from this ERGIC fraction was shown to be required for LC3 lipidation (Ge et al, 2014). These observations suggested that, in higher eukaryotes, the COPII vesicles used in autophagy are spatially separated from those that traffic to the Golgi.…”

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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Section: Discussionmentioning

confidence: 99%

Sec24 phosphorylation regulates autophagosome abundance during nutrient deprivation

Davis

Wang

Zhu

et al. 2016

eLife

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“…ER-derived transport intermediates fuse with acceptor membranes through a series of targeting and fusion events that also rely on a highly conserved machinery 28 . In general, membrane targeting depends on RAB GTPases that function in concert with extended coiled-coil domain proteins, such as p115 (known as Uso1 in yeast), as well as the multisubunit TRAPPI (transport protein particle I) complex 29–31 .…”

Section: Basic Elements Of the Er–golgi Interfacementioning

confidence: 99%

Organization of the ER–Golgi interface for membrane traffic control

Brandizzí

Barlowe

2013

Nat Rev Mol Cell Biol

457

471

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Coat protein complex I (COPI) and COPII are required for bidirectional membrane trafficking between the endoplasmic reticulum (ER) and the Golgi. While these core coat machineries and other transport factors are highly conserved across species, high-resolution imaging studies indicate that the organization of the ER–Golgi interface is varied in eukaryotic cells. Regulation of COPII assembly, in some cases to manage distinct cellular cargo, is emerging as one important component in determining this structure. Comparison of the ER–Golgi interface across different systems, particularly mammalian and plant cells, reveals fundamental elements and distinct organization of this interface. A better understanding of how these interfaces are regulated to meet varying cellular secretory demands should provide key insights into the mechanisms that control efficient trafficking of proteins and lipids through the secretory pathway.

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“…Transport through the early secretory pathway relies on another set of coated vesicular intermediates known as coatamer protein complex I (COPI)-coated vesicles (see Lorente-Rodriguez and Barlowe 2011;Wieland 2011). The COPI coat consists of seven proteins that form a multiprotein complex, much like the COPII coat (Lee and Goldberg 2010), which, together with the small GTPase ARF1 decorates vesicular intermediates primarily formed at the Golgi.…”

Section: Brefeldin a Resistancementioning

confidence: 99%