Vacuole membrane protein 1, autophagy and much more

Calvo‐Garrido, Javier; Carilla-Latorre, Sergio; Escalante, Ricardo

doi:10.4161/auto.6574

Cited by 25 publications

(38 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The pleiotropic defects associated with VMP1 depletion in model organisms suggested a more general function for this protein [38]. Our studies may now explain the apparently disparate phenotypes observed in different organelles such as mitochondria and chloroplasts in Chlamydomonas [26]; ER, Golgi and contractile vacuole in Dictyostelium [18], and processes as diverse as cytokinesis, secretion and endocytosis [18, 20, 26, 39, 40].…”

Section: Discussionmentioning

confidence: 75%

VMP1 Establishes ER-Microdomains that Regulate Membrane Contact Sites and Autophagy

Tábara

Escalante

2016

PLoS ONE

Self Cite

View full text Add to dashboard Cite

The endoplasmic reticulum (ER) regulates organelle dynamics through the formation of membrane contact sites (MCS). Here we describe that VMP1, a multispanning ER-resident protein involved in autophagy, is enriched in ER micro-domains that are in close proximity to diverse organelles in HeLa and Cos-7 cells. These VMP1 puncta are highly dynamic, moving in concert with lipid droplets, mitochondria and endosomes. Some of these micro-domains are associated with ER sliding events and also with fission events of mitochondria and endosomes. VMP1-depleted cells display increased ER-mitochondria MCS and altered mitochondria morphology demonstrating a role in the regulation of MCS. Additional defects in ER structure and lipid droplets size and distribution are consistent with a more general function of VMP1 in membrane remodeling and organelle function. We hypothesize that in autophagy VMP1 is required for the correct morphogenesis of the omegasome by regulating MCS at the site of autophagosome formation.

show abstract

Section: Discussionmentioning

confidence: 75%

VMP1 Establishes ER-Microdomains that Regulate Membrane Contact Sites and Autophagy

Tábara

Escalante

2016

PLoS ONE

Self Cite

View full text Add to dashboard Cite

show abstract

“…The localization of Vmp1 to the ER and its partial colocalization with autophagosomes are in line with other studies that suggest the involvement of the ER in autophagy. [96][97][98][99] Atg18 interacts with Atg2, and this complex is localized to the autophagosome membrane via Atg18 binding to PtdIns(3)P, through the novel conserved motif FRRG. 64,65 This localization is essential for the recruitment of other autophagic proteins and for autophagy, although the precise function of these proteins is unknown.…”

Section: Monitoring Autophagy In Dictyosteliummentioning

confidence: 99%

Autophagy in Dictyostelium: Genes and pathways, cell death and infection

Calvo‐Garrido¹,

Carilla-Latorre²,

Kubohara³

et al. 2010

Autophagy

Self Cite

View full text Add to dashboard Cite

“…74 Autophagy is important in both multicellular development and in the phagocytosis and digestion of bacterial prey. Intriguingly, the molecular analysis of autophagy in D. discoideum suggests that in this protist the core features of macroautophagy retain some interactions that are otherwise thought to occur only in yeast (Atg17-dependency, 14 see the previous section), to occur only in yeast and plants (Atg13-dependency) or to occur in mammals but not yeast (VMP1-dependency 75,76 ). In addition, some Dictyostelium ATG proteins exhibit structural architectures that are more reminiscent of animal homologues than they are of yeast homologues (ATG1, ATG16).…”

Section: Functional Analyses Of Autophagy In Free-living Protistsmentioning

confidence: 99%

“…69,75,76 As in mammalian cells, this protein, which is absent from yeast, is multifunctional and found at different intracellular locations making it difficult to assess whether the effect of VMP1 deletion on autophagy is direct or a pleiotropic consequence of losing a protein involved in numerous cellular processes. There is, however, some evidence that VMP1 in Dictyostelium is present in autophagosomes.…”

confidence: 99%

Autophagy in protists

et al. 2011

View full text Add to dashboard Cite

Autophagy is the degradative process by which eukaryotic cells digest their own components using acid hydrolases within the lysosome. Originally thought to function almost exclusively in providing starving cells with nutrients taken from their own cellular constituents, autophagy is in fact involved in numerous cellular events including differentiation, turnover of macromolecules and organelles, and defense against parasitic invaders. During the last 10-20 years, molecular components of the autophagic machinery have been discovered, revealing a complex interactome of proteins and lipids, which, in a concerted way, induce membrane formation to engulf cellular material and target it for lysosomal degradation. Here, our emphasis is autophagy in protists. We discuss experimental and genomic data indicating that the canonical autophagy machinery characterized in animals and fungi appeared prior to the radiation of major eukaryotic lineages. Moreover, we describe how comparative bioinformatics revealed that this canonical machinery has been subject to moderation, outright loss or elaboration on multiple occasions in protist lineages, most probably as a consequence of diverse lifestyle adaptations. We also review experimental studies illustrating how several pathogenic protists either utilize autophagy mechanisms or manipulate host-cell autophagy in order to establish or maintain infection within a host. The essentiality of autophagy for the pathogenicity of many parasites, and the unique features of some of the autophagy-related proteins involved, suggest possible new targets for drug discovery. Further studies of the molecular details of autophagy in protists will undoubtedly enhance our understanding of the diversity and complexity of this cellular phenomenon and the opportunities it offers as a drug target

show abstract

Vacuole membrane protein 1, autophagy and much more

Cited by 25 publications

References 21 publications

VMP1 Establishes ER-Microdomains that Regulate Membrane Contact Sites and Autophagy

VMP1 Establishes ER-Microdomains that Regulate Membrane Contact Sites and Autophagy

Autophagy in Dictyostelium: Genes and pathways, cell death and infection

Autophagy in protists

Contact Info

Product

Resources

About