<i><scp>ATG</scp>15</i> encodes a phospholipase and is transcriptionally regulated by <scp>YAP</scp>1 in <i>Saccharomyces cerevisiae</i>

Ramya, Visvanathan; Rajasekharan, Ram

doi:10.1002/1873-3468.12369

Cited by 35 publications

(36 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition to these broader issues, many questions still remain about Atg15 itself (Box 1). Atg15 is a vacuolar phospholipase that has activity primarily towards phosphotidylserine and, to a lesser extent, cardiolipin and phosphatidylethanolamine [33,34]. As mentioned above, Atg15 is required for efficient turnover of LDs within the vacuole [28].…”

Section: Lipidsmentioning

confidence: 99%

Vacuolar hydrolysis and efflux: current knowledge and unanswered questions

Parzych

Klionsky

2018

Autophagy

View full text Add to dashboard Cite

Hydrolysis within the vacuole in yeast and the lysosome in mammals is required for the degradation and recycling of a multitude of substrates, many of which are delivered to the vacuole/lysosome by autophagy. In humans, defects in lysosomal hydrolysis and efflux can have devastating consequences, and contribute to a class of diseases referred to as lysosomal storage disorders. Despite the importance of these processes, many of the proteins and regulatory mechanisms involved in hydrolysis and efflux are poorly understood. In this review, we describe our current knowledge of the vacuolar/lysosomal degradation and efflux of a vast array of substrates, focusing primarily on what is known in the yeast Saccharomyces cerevisiae. We also highlight many unanswered questions, the answers to which may lead to new advances in the treatment of lysosomal storage disorders.

show abstract

Section: Lipidsmentioning

confidence: 99%

Vacuolar hydrolysis and efflux: current knowledge and unanswered questions

Parzych

Klionsky

2018

Autophagy

View full text Add to dashboard Cite

show abstract

“…The best-known and described protein involved in the degradation of the autophagic body in yeast is Atg15, a putative lipase (Figure 2, Table 3). It has been proven that this protein plays a role in the degradation of the autophagic body, not only through the decomposition and recycling of components of the autophagic body membrane but also due to it being a key protein involved in the degradation of the cargo located inside the autophagic body [34,[117][118][119][120]. In addition to those described above, there are several other proteins that are thought to be involved in the degradation of the autophagic body in yeast, but their mechanism of action and functions are not yet fully understood.…”

Section: Degradation Of the Autophagic Body And Metabolite Efflux Fromentioning

confidence: 99%

“…Pep4 (Proteinase A), Prb1 (Proteinase B) yeast activation of protease and hydrolase cascades by proteolytic processing [34,115,116] Atg15, yeast degradation of autophagic body, decomposition and recycling of autophagic body membrane, proaminopeptidase I maturation [34,[117][118][119][120] Atg22 yeast tonoplast protein with limited homology to permeases, putative vacuolar transporter involved in the efflux of metabolites from the vacuole to the cytoplasm [122,123] Atg42, Ybr139, Prc1 yeast probably degradation of the autophagic body [56] Avt3…”

Section: Organism Function Referencesmentioning

confidence: 99%

Completing Autophagy: Formation and Degradation of the Autophagic Body and Metabolite Salvage in Plants

Stefaniak

Wojtyla

Pietrowska‐Borek

et al. 2020

IJMS

View full text Add to dashboard Cite

Autophagy is an evolutionarily conserved process that occurs in yeast, plants, and animals. Despite many years of research, some aspects of autophagy are still not fully explained. This mostly concerns the final stages of autophagy, which have not received as much interest from the scientific community as the initial stages of this process. The final stages of autophagy that we take into consideration in this review include the formation and degradation of the autophagic bodies as well as the efflux of metabolites from the vacuole to the cytoplasm. The autophagic bodies are formed through the fusion of an autophagosome and vacuole during macroautophagy and by vacuolar membrane invagination or protrusion during microautophagy. Then they are rapidly degraded by vacuolar lytic enzymes, and products of the degradation are reused. In this paper, we summarize the available information on the trafficking of the autophagosome towards the vacuole, the fusion of the autophagosome with the vacuole, the formation and decomposition of autophagic bodies inside the vacuole, and the efflux of metabolites to the cytoplasm. Special attention is given to the formation and degradation of autophagic bodies and metabolite salvage in plant cells.

show abstract

“…However, given that the membraneembedded remodeled GPI anchor contains long chain fatty acids or ceramide, it is likely that additional mechanisms such as invaginations or membrane recycling must exist in order to maintain vacuolar membrane lipid homeostasis. Intravacuolar membrane-bound structures like microautophagic vesicles, Cvt vesicles, autophagic bodies and ILVs are rapidly dissolved by the action of Atg15, a vacuolar lipase (Teter et al, 2001;Ramya and Rajasekharan, 2016). As such, an intravacuolar vesicle that originates from invagination from the vacuolar membrane is likely also sensitive to Atg15.…”

Section: Pep4-dependent Protein Internalization From the Vacuolar Memmentioning

confidence: 99%

A post-ER degradation pathway that relies on protease-dependent internalization from the vacuolar membrane

Lemus

Matić

Goder

2019

Preprint

View full text Add to dashboard Cite

2 Abbreviations: GPI anchor: glycosylphophatidylinositol anchor; ESCRT: endosomal sorting complexes required for transport; MVBs: multi vesicular bodies; ILVs: intraluminal vesicles; ERAD: endoplasmic reticulum-associated protein degradation; TMD: transmembrane domain; PVC: prevacuolar compartment; SNARE: soluble NSF attachment protein receptor; Cvt vesicle: cytoplasm to vacuole targeting vesicle Keywords: Protein degradation, secretory pathway, vacuole, vacuolar protease, membrane invagination Highlights: • ER-exited misfolded GPI-anchored proteins are routed to the vacuole via endosomes but do not internalize into intraluminal vesicles • Internalization occurs directly from the vacuolar membrane into intravacuolar mobile structures • Internalization from the vacuolar membrane depends on the proteolytic activity of the vacuolar protease Pep4 3 Summary Newly synthesized proteins of the secretory pathway are quality-controlled inside the endoplasmic reticulum (ER) and, if not properly folded, are retained. An exception are glycosylphosphatidylinositol-anchored proteins (GPI-APs) which can leave the ER even when misfolded and are routed to the vacuole/lysosome for degradation by largely unknown mechanisms linked to post-ER quality control. Using yeast as model organism,we show that Gas1*, an ER-exported misfolded GPI-AP, is diverted from the secretory pathway to endosomes for transport to the vacuole. However, Gas1* is not sorted into endosomal intraluminal vesicles but internalizes directly from the vacuolar membrane.There, the vacuolar protease Pep4, but not any other known vacuolar protease, is required for Gas1* internalization. Our data reveal novel and unexpected mechanisms for invaginations from the vacuolar membrane.

show abstract

ATG15 encodes a phospholipase and is transcriptionally regulated by YAP1 in Saccharomyces cerevisiae

Cited by 35 publications

References 46 publications

Vacuolar hydrolysis and efflux: current knowledge and unanswered questions

Vacuolar hydrolysis and efflux: current knowledge and unanswered questions

Completing Autophagy: Formation and Degradation of the Autophagic Body and Metabolite Salvage in Plants

A post-ER degradation pathway that relies on protease-dependent internalization from the vacuolar membrane

Contact Info

Product

Resources

About