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  1. Article ; Online: Phagophore-lysosome/vacuole fusion in mutant yeast and mammalian cells.

    Liang, Yongheng

    Autophagy

    2023  Volume 19, Issue 9, Page(s) 2595–2600

    Abstract: Macroautophagy/autophagy is a process through which the phagophores engulf non-essential or damaged cellular materials, forming double-membrane autophagosomes (APs) and fusing with lysosomes/vacuoles, after which the materials are degraded for recycling ... ...

    Abstract Macroautophagy/autophagy is a process through which the phagophores engulf non-essential or damaged cellular materials, forming double-membrane autophagosomes (APs) and fusing with lysosomes/vacuoles, after which the materials are degraded for recycling purposes. Autophagy is associated with increased cell survival under different stress conditions. AP-lysosome/vacuole fusion is a critical step in autophagy. Some mutant cells can accumulate phagophores under autophagy-induction conditions. Autophagy is interrupted when accumulated phagophores cannot fuse with lysosomes/vacuoles, resulting in a significant decrease in cell survivability. However, phagophore-lysosome/vacuole fusion has been reported in related mammalian cells and yeast mutant cells. This observation indicates that it is possible to restore a partial autophagy process after interruption. Furthermore, these findings indicate that phagophore closure is not a prerequisite for its fusion with the lysosome/vacuole in the mutant cells. The phagophore-lysosome/vacuole fusion strategy can significantly rescue defective autophagy due to failed phagophore closure. This commentary discusses the fusion of phagophores and lysosomes/vacuoles and implications of such fusion events.
    MeSH term(s) Animals ; Autophagosomes/metabolism ; Vacuoles/metabolism ; Saccharomyces cerevisiae/genetics ; Autophagy/genetics ; Lysosomes/metabolism ; Membrane Fusion ; Mammals
    Language English
    Publishing date 2023-04-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2023.2205272
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  2. Article: Phagophore Closure.

    Liang, Yongheng

    Advances in experimental medicine and biology

    2021  Volume 1208, Page(s) 43–53

    Abstract: Phagophore closure is a critical step during macroautophagy. However, the proteins and mechanisms to regulate this step have been elusive for a long time. In 2017, Rab5 was affirmed to play a role in phagophore closure in yeast. Furthermore, in mammalian ...

    Abstract Phagophore closure is a critical step during macroautophagy. However, the proteins and mechanisms to regulate this step have been elusive for a long time. In 2017, Rab5 was affirmed to play a role in phagophore closure in yeast. Furthermore, in mammalian cells, ESCRT III was reported to have roles in phagophore closure and mitophagosome closure in vivo in 2018 and 2019, respectively. The role of ESCRT in phagophore closure was confirmed in yeast, both in vivo and in vitro, in 2019. Most importantly, the latter paper found that Atg17 recruited the ESCRT III subunit Snf7 to the phagophore to close it under the control of Rab5. To determine the closure characteristics of autophagosome-like membrane structures in ESCRT mutants, a traditional protease protection assay with immunoblotting was used, accompanied by new techniques that were developed, including immunofluorescence assays, autophagosome completion assays, and the optogenetic closure assay. This study delivered our current understanding of phagophore closure and provided more reference methods to detect membrane closure.
    MeSH term(s) Animals ; Autophagosomes ; Autophagy ; Endosomal Sorting Complexes Required for Transport ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics
    Chemical Substances Endosomal Sorting Complexes Required for Transport ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2021-07-14
    Publishing country United States
    Document type Journal Article
    ISSN 2214-8019 ; 0065-2598
    ISSN (online) 2214-8019
    ISSN 0065-2598
    DOI 10.1007/978-981-16-2830-6_3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Vtc4 Promotes the Entry of Phagophores into Vacuoles in the

    Chen, Xiaofan / Liang, Yongheng

    Journal of fungi (Basel, Switzerland)

    2023  Volume 9, Issue 10

    Abstract: Endocytosis and autophagy are the main pathways to deliver cargoes in vesicles and autophagosomes, respectively, to vacuoles/lysosomes in eukaryotes. Multiple positive regulators but few negative ones are reported to regulate the entry of vesicles and ... ...

    Abstract Endocytosis and autophagy are the main pathways to deliver cargoes in vesicles and autophagosomes, respectively, to vacuoles/lysosomes in eukaryotes. Multiple positive regulators but few negative ones are reported to regulate the entry of vesicles and autophagosomes into vacuoles/lysosomes. In yeast, the Rab5 GTPase Vps21 and the ESCRT (endosomal sorting complex required for transport) are positive regulators in endocytosis and autophagy. During autophagy, Vps21 regulates the ESCRT to phagophores (unclosed autophagosomes) to close them. Phagophores accumulate on vacuolar membranes in both
    Language English
    Publishing date 2023-10-11
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2784229-0
    ISSN 2309-608X ; 2309-608X
    ISSN (online) 2309-608X
    ISSN 2309-608X
    DOI 10.3390/jof9101003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Using GBP Nanotrap to Restore Autophagy in the Rab5/Vps21 Mutant by Forcing Snf7 and Atg17 Interaction.

    Zhao, Mengzhu / Liang, Yongheng

    Methods in molecular biology (Clifton, N.J.)

    2021  Volume 2293, Page(s) 181–188

    Abstract: Protein-protein interactions are important for physiology performance. Green fluorescent protein (GFP) is a widely used protein tag to show protein localization in vivo. GFP binding protein (GBP) is a specific domain with high affinity to GFP. A novel ... ...

    Abstract Protein-protein interactions are important for physiology performance. Green fluorescent protein (GFP) is a widely used protein tag to show protein localization in vivo. GFP binding protein (GBP) is a specific domain with high affinity to GFP. A novel technique with GBP fused protein X tagged with red fluorescence protein binding to GFP of GFP fused protein Y to establish a close association for proteins X and Y independently from other proteins has recently been developed. It is found that the interaction and colocalization between Snf7 and Atg17 is impaired in Saccharomyces cerevisiae vps21Δ cells, which are defective in autophagy. In order to determine whether the interaction between Snf7 and Atg17 is important for autophagy, we forced the interaction between Snf7 and Atg17 through GBP-GFP binding. Snf7-GBP-mCherry and/or GFP-Atg17 tagged wild-type and vps21Δ cells were compared for autophagy process under starvation by determining the maturation of proprotein of Ape1 (prApe1). Our results showed that the defective autophagy in vps21Δ cells was significantly suppressed when both Snf7-GBP-mCherry and GFP-Atg17 were installed. Our results indicate that the GBP-GFP nanotrap technique is a powerful tool to restore colocalization/interaction in vivo and the Snf7-Atg17 interaction is important for yeast autophagy.
    MeSH term(s) Autophagy/genetics ; Autophagy-Related Proteins/metabolism ; Endosomal Sorting Complexes Required for Transport ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Protein Transport ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; rab GTP-Binding Proteins/genetics ; rab5 GTP-Binding Proteins
    Chemical Substances Atg17 protein, S cerevisiae ; Autophagy-Related Proteins ; Endosomal Sorting Complexes Required for Transport ; SNF7 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Green Fluorescent Proteins (147336-22-9) ; VPS21 protein, S cerevisiae (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2) ; rab5 GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2021-08-28
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-1346-7_12
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Yeast phospholipase D, Spo14, is not required for macroautophagy

    Chen, Yun / Wu, Zulin / Dong, Lin / You, Xia / Ji, Yanling / Liang, Yongheng

    Yeast. 2022 June, v. 39, no. 6-7

    2022  

    Abstract: Autophagy‐related gene (Atg) proteins are key players in autophagy. Some proteins that function in vesicle trafficking and lipid metabolism are also involved in autophagy. The SPO14 in yeast, which encodes phospholipase D (PLD), is involved in membrane ... ...

    Abstract Autophagy‐related gene (Atg) proteins are key players in autophagy. Some proteins that function in vesicle trafficking and lipid metabolism are also involved in autophagy. The SPO14 in yeast, which encodes phospholipase D (PLD), is involved in membrane trafficking and plays a vital role in sporulation during meiosis. Crosstalk has been identified between autophagy and sporulation. Although the PLD is required for macroautophagy in mammals, its role in yeast macroautophagy remains unclear. We observed that Spo14 is not required for macroautophagy in yeast and that it is dispensable for Atg8 lipidation, which plays an important role in phagophore extension. Our results also revealed that green fluorescent protein (GFP)‐Atg8 degradation is not completely blocked in atg1Δ/atg1Δ cells under sporulation condition. Therefore, Spo14 is not required for macroautophagy in yeast.
    Keywords genes ; green fluorescent protein ; lipid metabolism ; macroautophagy ; meiosis ; phospholipases ; sporulation ; yeasts
    Language English
    Dates of publication 2022-06
    Size p. 401-411.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 632636-5
    ISSN 1097-0061 ; 0749-503X
    ISSN (online) 1097-0061
    ISSN 0749-503X
    DOI 10.1002/yea.3803
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: The endosomal sorting complex required for transport complex negatively regulates Erg6 degradation under specific glucose restriction conditions.

    Zhang, Ao / Meng, Ying / Li, Qunli / Liang, Yongheng

    Traffic (Copenhagen, Denmark)

    2020  Volume 21, Issue 7, Page(s) 488–502

    Abstract: Lipid droplets (LDs) are cytosolic fat storage organelles that play roles in lipid metabolism, trafficking and signaling. Breakdown of LDs in Saccharomyces cerevisiae is mainly achieved by lipolysis and lipophagy. In this study, we found that the ... ...

    Abstract Lipid droplets (LDs) are cytosolic fat storage organelles that play roles in lipid metabolism, trafficking and signaling. Breakdown of LDs in Saccharomyces cerevisiae is mainly achieved by lipolysis and lipophagy. In this study, we found that the endosomal sorting complex required for transport (ESCRT) in S. cerevisiae negatively regulated the turnover of a LD marker, Erg6, under both simplified glucose restriction (GR) and acute glucose restriction (AGR) conditions by monitoring the localization and degradation of Erg6. Loss of Vps27, Snf7 or Vps4, representative subunits of the ESCRT machinery, facilitated the delivery of Erg6-GFP to vacuoles and its degradation depending on the lipophagy protein Atg15 under simplified GR. Additionally, the lipolysis proteins Tgl3 and Tgl4 were also involved in the enhanced vacuolar localization and degradation of Erg6-GFP in vps4Δ cells. Furthermore, we found that Atg14, which is required for the formation of putatively liquid-ordered (Lo) membrane domains on the vacuole that act as preferential internalization sites for LDs, abundantly localized to vacuolar membranes in ESCRT mutants. Most importantly, the depletion or overexpression of Atg14 correspondingly abolished or promoted the observed Erg6 degradation in ESCRT mutant cells. We propose that Atg14 together with other proteins promotes Erg6 degradation in ESCRT mutant cells under specific glucose restriction conditions. These results shed new light on the regulation of ESCRT on LD turnover.
    MeSH term(s) Adenosine Triphosphatases ; Endosomal Sorting Complexes Required for Transport/metabolism ; Glucose/metabolism ; Methyltransferases ; Protein Transport ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Endosomal Sorting Complexes Required for Transport ; Saccharomyces cerevisiae Proteins ; VPS27 protein, S cerevisiae ; VPS4 protein, S cerevisiae ; Methyltransferases (EC 2.1.1.-) ; delta 24-sterol methyltransferase (EC 2.1.1.41) ; Adenosine Triphosphatases (EC 3.6.1.-) ; Glucose (IY9XDZ35W2)
    Language English
    Publishing date 2020-05-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12732
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5634: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  7. Article ; Online: The ESCRT-III complex contributes to macromitophagy in yeast.

    Wu, Zulin / Xu, Haiqian / Liu, Junze / Zhou, Fan / Liang, Yongheng

    Traffic (Copenhagen, Denmark)

    2021  Volume 22, Issue 8, Page(s) 258–273

    Abstract: Mitochondria play important roles in energy generation and homeostasis maintenance in eukaryotic cells. The damaged or superfluous mitochondria can be nonselectively or selectively removed through the autophagy/lysosome pathway, which was referred as ... ...

    Abstract Mitochondria play important roles in energy generation and homeostasis maintenance in eukaryotic cells. The damaged or superfluous mitochondria can be nonselectively or selectively removed through the autophagy/lysosome pathway, which was referred as mitophagy. According to the molecular machinery for degrading mitochondria, the selectively removed mitochondria can occur through macromitophagy or micromitophagy. In this study, we show that the endosomal sorting complex required for transport III (ESCRT-III) in budding yeast regulates macromitophagy induced by nitrogen starvation, but not by the post-logarithmic phase growth in lactate medium by monitoring a mitochondrial marker, Om45. Firstly, loss of ESCRT-III subunit Snf7 or Vps4-Vta1 complex subunit Vps4, two representative subunits of the ESCRT complex, suppresses the delivery and degradation of Om45-GFP to vacuoles. Secondly, we show that the mitochondrial marker Om45 and mitophagy receptor Atg32 accumulate on autophagosomes marked with Atg8 (mitophagosomes, MPs) in ESCRT mutants. Moreover, the protease-protection assay indicates that Snf7 and Vps4 are involved in MP closure. Finally, Snf7 interacts with Atg11, which was detected by two ways, glutathione-S-transferase (GST) pulldown and bimolecular fluorescence complementation (BiFC) assay, and this BiFC interaction happens on mitochondrial reticulum. Therefore, we proposed that the ESCRT-III machinery mediates nitrogen starvation-induced macromitophagy by the interaction between Snf7 and Atg11 so that Snf7 is recruited to Atg32-marked MPs by the known Atg11-Atg32 interaction to seal them. These results reveal that the ESCRT-III complex plays a new role in yeast on macromitophagy.
    MeSH term(s) Adenosine Triphosphatases ; Autophagosomes ; Autophagy-Related Proteins/genetics ; Endosomal Sorting Complexes Required for Transport/genetics ; Mitophagy ; Receptors, Cytoplasmic and Nuclear ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics
    Chemical Substances Atg32 protein, S cerevisiae ; Autophagy-Related Proteins ; Endosomal Sorting Complexes Required for Transport ; Receptors, Cytoplasmic and Nuclear ; Saccharomyces cerevisiae Proteins ; VPS4 protein, S cerevisiae ; VTA1 protein, S cerevisiae ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2021-06-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12805
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    ab Jg. 2022: Lesesaal (EG)

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  8. Article ; Online: Yeast phospholipase D, Spo14, is not required for macroautophagy.

    Chen, Yun / Wu, Zulin / Dong, Lin / You, Xia / Ji, Yanling / Liang, Yongheng

    Yeast (Chichester, England)

    2022  Volume 39, Issue 6-7, Page(s) 401–411

    Abstract: Autophagy-related gene (Atg) proteins are key players in autophagy. Some proteins that function in vesicle trafficking and lipid metabolism are also involved in autophagy. The SPO14 in yeast, which encodes phospholipase D (PLD), is involved in membrane ... ...

    Abstract Autophagy-related gene (Atg) proteins are key players in autophagy. Some proteins that function in vesicle trafficking and lipid metabolism are also involved in autophagy. The SPO14 in yeast, which encodes phospholipase D (PLD), is involved in membrane trafficking and plays a vital role in sporulation during meiosis. Crosstalk has been identified between autophagy and sporulation. Although the PLD is required for macroautophagy in mammals, its role in yeast macroautophagy remains unclear. We observed that Spo14 is not required for macroautophagy in yeast and that it is dispensable for Atg8 lipidation, which plays an important role in phagophore extension. Our results also revealed that green fluorescent protein (GFP)-Atg8 degradation is not completely blocked in atg1Δ/atg1Δ cells under sporulation condition. Therefore, Spo14 is not required for macroautophagy in yeast.
    MeSH term(s) Animals ; Autophagy/genetics ; Autophagy/physiology ; Autophagy-Related Protein 8 Family/genetics ; Autophagy-Related Protein 8 Family/metabolism ; Macroautophagy ; Mammals ; Meiosis ; Phospholipase D/genetics ; Phospholipase D/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Autophagy-Related Protein 8 Family ; Saccharomyces cerevisiae Proteins ; Phospholipase D (EC 3.1.4.4) ; SPO14 protein, S cerevisiae (EC 3.1.4.4)
    Language English
    Publishing date 2022-06-27
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 632636-5
    ISSN 1097-0061 ; 0749-503X
    ISSN (online) 1097-0061
    ISSN 0749-503X
    DOI 10.1002/yea.3803
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    Zs.B 2820: Show issues Location:
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  9. Article ; Online: Trs20, Trs23, Trs31 and Bet5 participate in autophagy through GTPase Ypt1 in Saccharomyces cerevisiae

    Zou Shenshen / Liu Yan / Min Gaoyi / Liang Yongheng

    Archives of Biological Sciences, Vol 70, Iss 1, Pp 109-

    2018  Volume 118

    Abstract: TRAPP (transport protein particle) is a large, highly conserved, multi-subunit complex. Four types of TRAPP complexes (I, II, III and most recently IV) have been identified in Saccharomyces cerevisiae. Studies on the roles of TRAPP II, TRAPP III and ... ...

    Abstract TRAPP (transport protein particle) is a large, highly conserved, multi-subunit complex. Four types of TRAPP complexes (I, II, III and most recently IV) have been identified in Saccharomyces cerevisiae. Studies on the roles of TRAPP II, TRAPP III and TRAPP IV specific subunits (Trs130, Trs85 and Trs33) have demonstrated that TRAPP II, TRAPP III and TRAPP IV activate the small GTPases that regulate autophagy. Up to now, the roles of the common TRAPP subunits have been well studied in vesicle transport. However, the roles of the common TRAPP subunits and their relationship to Ypt/Rab GTPases in autophagy are not clear. In this paper, we examined Trs20, Trs23, Trs31, and Bet5 (the common TRAPP subunits), which are required for starvation-induced autophagy and the cytoplasm-to-vacuole targeting (Cvt) pathway. During autophagy, GFP-Atg8 accumulates as single or multiple dots and is not recruited into the pre-autophagosomal structures (PAS) in trs20ts, trs23ts, trs31ts and bet5ts mutant cells. Furthermore, these dots are linked to the endoplasmic reticulum in mutant cells. Additionally, overexpression of Ypt1, but not Ypt31, suppresses the autophagy defect in trs20ts, trs23ts, trs31ts and bet5ts mutant cells. Based on these results, we concluded that Trs20, Trs23, Trs31, and Bet5 are required for autophagy, and that these common TRAPP subunits regulate autophagy partially through GTPase Ypt1, but not Ypt31.
    Keywords autophagy ; TRAPP ; common TRAPP subunits ; Ypt1 ; Ypt31 ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2018-01-01T00:00:00Z
    Publisher University of Belgrade, University of Novi Sad
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Vrl1 relies on its VPS9-domain to play a role in autophagy in Saccharomyces cerevisiae.

    Li, Wenjing / Wu, Zulin / Liang, Yongheng

    Cell biology international

    2019  Volume 43, Issue 8, Page(s) 875–889

    Abstract: Autophagy is an intracellular degradation process involving many Atg proteins, which are recruited hierarchically to regulate this process. Rab/Ypt GTPases and their activators, guanine nucleotide exchange factors (GEFs), which are critical for ... ...

    Abstract Autophagy is an intracellular degradation process involving many Atg proteins, which are recruited hierarchically to regulate this process. Rab/Ypt GTPases and their activators, guanine nucleotide exchange factors (GEFs), which are critical for regulating vesicle trafficking, are also involved in autophagy. Previously, we reported that yeast Vps21 and its GEF Vps9 are required for autophagy. Later, a third yeast VPS9-domain-containing protein, VARP-like 1 (Vrl1), which was identified as a mutant in major laboratory strains, had partially overlapping functions with Vps9 in trafficking. In this study, we showed that Vrl1 performed roles in autophagy, and its VPS9-domain was crucial for its role in autophagy. We found that localization of Vrl1 differed from the other two VPS9-domain-containing proteins, Vps9 and Muk1, and only Vrl1 changed from multipoint to diffusion after starvation. Like Vps9, Vrl1 suppressed autophagic defects caused by the VPS9 deletion. We further showed that these VPS9-domain-containing proteins, Vps9, Muk1, and Vrl1, all co-localized with Atg8 on autophagosomes in cells blocked in any late step of starvation-induced autophagy, with Vrl1 most often co-localizing with Atg8. A small portion (<25%) of these VPS9-domain-containing proteins were degraded through autophagy. However, a large portion (>60%) of Vrl1 decreased independently of autophagy. We propose that Vrl1 may regulate autophagy in a similar way as Vps9, and the level of Vrl1 partly decreases through both autophagy-dependent and -independent routes.
    MeSH term(s) Autophagy ; Autophagy-Related Protein 8 Family/metabolism ; Autophagy-Related Proteins/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Protein Domains ; Protein Transport ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Vacuoles/metabolism ; Vesicular Transport Proteins/metabolism ; rab GTP-Binding Proteins/metabolism
    Chemical Substances ATG8 protein, S cerevisiae ; Autophagy-Related Protein 8 Family ; Autophagy-Related Proteins ; Guanine Nucleotide Exchange Factors ; Muk1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; VPS9 protein, S cerevisiae ; Vesicular Transport Proteins ; Vrl1 protein, S cerevisiae ; VPS21 protein, S cerevisiae (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2019-05-20
    Publishing country England
    Document type Journal Article
    ZDB-ID 1143453-3
    ISSN 1095-8355 ; 1065-6995
    ISSN (online) 1095-8355
    ISSN 1065-6995
    DOI 10.1002/cbin.11156
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1451: Show issues Location:
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