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  1. AU="Zhao, Sarah F"
  2. AU=Zhang Yeqian AU=Zhang Yeqian
  3. AU="Goble, Carole"
  4. AU="Rowe, Laura"
  5. AU="Vottonen, Linda"
  6. AU="Citron, Diane M"
  7. AU="Doruk, Sibel"
  8. AU="Aransay, Ana M"
  9. AU="Dobbs, Katherine R"
  10. AU=Sinha Surabhi
  11. AU="K Siaw-Acheampong"
  12. AU="Ni, Zhao-Hui"
  13. AU="Sanderson, J. Thomas"
  14. AU="Raynaud, F I"
  15. AU="Jin, Di"
  16. AU="Raguzin, E" AU="Raguzin, E"
  17. AU="Rico, Alex"
  18. AU="Grinspan, Judith B"
  19. AU="Doerler, M"
  20. AU="Nyland, P"
  21. AU="Rana, Jigyasa"
  22. AU="Fennimore, Laura"
  23. AU="Blankstein, Kenneth"
  24. AU="O' Callaghan, Carol"
  25. AU="Van Snick, Jacques"
  26. AU="Yao, Xiaobin"
  27. AU="Georg Häcker"
  28. AU="Jain, S."
  29. AU="Alfakir, Razan"
  30. AU="Sozbilir, U."
  31. AU=Zhang Shuanghong
  32. AU="Iwama, Hisakazu"
  33. AU="Gomes, Andreia"
  34. AU="Machuca, Víctor"
  35. AU=Liu Nanyang AU=Liu Nanyang
  36. AU="Boudina, Sihem"
  37. AU="Ma, DongXue"
  38. AU="Bellucci, Margherita"
  39. AU="Prima, Musharrat Jahan"
  40. AU="Saiegh, Fadi Al"
  41. AU="Yang, Deok-Chun"
  42. AU="Arima, Hisatomi"
  43. AU=Czubak Jacek
  44. AU="de Melo, Bruna Oliveira"
  45. AU="Sokhadze, Guela"
  46. AU="Meuleman, Philip"
  47. AU=Mishra Arnab Kumar AU=Mishra Arnab Kumar
  48. AU="Linda A. Gleaves"
  49. AU="Vandelli, Maria Angela"
  50. AU="Guerrera, Luigi Pio"
  51. AU="Sabitri Lamichhane"
  52. AU="Echevarria, Marco"
  53. AU="Yanmin Li"

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  1. Artikel ; Online: Dual function of Rab1A in secretion and autophagy: hypervariable domain dependence.

    Gyurkovska, Valeriya / Murtazina, Rakhilya / Zhao, Sarah F / Shikano, Sojin / Okamoto, Yukari / Segev, Nava

    Life science alliance

    2023  Band 6, Heft 5

    Abstract: We currently understand how the different intracellular pathways, secretion, endocytosis, and autophagy are regulated by small GTPases. In contrast, it is unclear how these pathways are coordinated to ensure efficient cellular response to stress. Rab ... ...

    Abstract We currently understand how the different intracellular pathways, secretion, endocytosis, and autophagy are regulated by small GTPases. In contrast, it is unclear how these pathways are coordinated to ensure efficient cellular response to stress. Rab GTPases localize to specific organelles through their hypervariable domain (HVD) to regulate discrete steps of individual pathways. Here, we explored the dual role of Rab1A/B (92% identity) in secretion and autophagy. We show that although either Rab1A or Rab1B is required for secretion, Rab1A, but not Rab1B, localizes to autophagosomes and is required early in stress-induced autophagy. Moreover, replacing the HVD of Rab1B with that of Rab1A enables Rab1B to localize to autophagosomes and regulate autophagy. Therefore, Rab1A-HVD is required for the dual functionality of a single Rab in two different pathways: secretion and autophagy. In addition to this mechanistic insight, these findings are relevant to human health because both the pathways and Rab1A/B were implicated in diseases ranging from cancer to neurodegeneration.
    Mesh-Begriff(e) Humans ; rab1 GTP-Binding Proteins/genetics ; rab1 GTP-Binding Proteins/metabolism ; Autophagy ; rab GTP-Binding Proteins/metabolism ; Autophagosomes/metabolism
    Chemische Substanzen rab1 GTP-Binding Proteins (EC 3.6.5.2) ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Sprache Englisch
    Erscheinungsdatum 2023-02-13
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 2575-1077
    ISSN (online) 2575-1077
    DOI 10.26508/lsa.202201810
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Characterization of constitutive ER-phagy of excess membrane proteins.

    Lipatova, Zhanna / Gyurkovska, Valeriya / Zhao, Sarah F / Segev, Nava

    PLoS genetics

    2020  Band 16, Heft 12, Seite(n) e1009255

    Abstract: Thirty percent of all cellular proteins are inserted into the endoplasmic reticulum (ER), which spans throughout the cytoplasm. Two well-established stress-induced pathways ensure quality control (QC) at the ER: ER-phagy and ER-associated degradation ( ... ...

    Abstract Thirty percent of all cellular proteins are inserted into the endoplasmic reticulum (ER), which spans throughout the cytoplasm. Two well-established stress-induced pathways ensure quality control (QC) at the ER: ER-phagy and ER-associated degradation (ERAD), which shuttle cargo for degradation to the lysosome and proteasome, respectively. In contrast, not much is known about constitutive ER-phagy. We have previously reported that excess of integral-membrane proteins is delivered from the ER to the lysosome via autophagy during normal growth of yeast cells. Whereas endogenously expressed ER resident proteins serve as cargos at a basal level, this level can be induced by overexpression of membrane proteins that are not ER residents. Here, we characterize this pathway as constitutive ER-phagy. Constitutive and stress-induced ER-phagy share the basic macro-autophagy machinery including the conserved Atgs and Ypt1 GTPase. However, induction of stress-induced autophagy is not needed for constitutive ER-phagy to occur. Moreover, the selective receptors needed for starvation-induced ER-phagy, Atg39 and Atg40, are not required for constitutive ER-phagy and neither these receptors nor their cargos are delivered through it to the vacuole. As for ERAD, while constitutive ER-phagy recognizes cargo different from that recognized by ERAD, these two ER-QC pathways can partially substitute for each other. Because accumulation of membrane proteins is associated with disease, and constitutive ER-phagy players are conserved from yeast to mammalian cells, this process could be critical for human health.
    Mesh-Begriff(e) Autophagy ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum-Associated Degradation ; Membrane Proteins/metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Stress, Physiological ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
    Chemische Substanzen Autophagy-Related Proteins ; Membrane Proteins ; Saccharomyces cerevisiae Proteins ; YPT1 protein, S cerevisiae (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Sprache Englisch
    Erscheinungsdatum 2020-12-04
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2186725-2
    ISSN 1553-7404 ; 1553-7390
    ISSN (online) 1553-7404
    ISSN 1553-7390
    DOI 10.1371/journal.pgen.1009255
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

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