Rab1a rescues the toxicity of PRAF3

The PRA1-superfamily member PRAF3 plays pivotal roles in membrane traffic as a GDI displacement factor via physical interaction with a variety of Rab proteins, as well as in the modulation of antioxidant glutathione through its interaction with EAAC1 (SLC1A1). Overproduction of PRAF3 is known to be...

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Autores principales: Oshikane, Hiroyuki, Watabe, Masahiko, Kikuchi-Utsumi, Kazue, Nakaki, Toshio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5986628/
https://www.ncbi.nlm.nih.gov/pubmed/29872729
http://dx.doi.org/10.1016/j.bbrep.2018.03.002
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author Oshikane, Hiroyuki
Watabe, Masahiko
Kikuchi-Utsumi, Kazue
Nakaki, Toshio
author_facet Oshikane, Hiroyuki
Watabe, Masahiko
Kikuchi-Utsumi, Kazue
Nakaki, Toshio
author_sort Oshikane, Hiroyuki
collection PubMed
description The PRA1-superfamily member PRAF3 plays pivotal roles in membrane traffic as a GDI displacement factor via physical interaction with a variety of Rab proteins, as well as in the modulation of antioxidant glutathione through its interaction with EAAC1 (SLC1A1). Overproduction of PRAF3 is known to be toxic to the host cells, although the factors capable of cancelling the toxicity remained unknown. We here show that Rab1a can rescue the cytotoxicity caused by PRAF3 possibly by “positively” regulating ER-Golgi trafficking, cancelling the “negative” modulation by PRAF3. Our results illuminate the close physiological relationship between PRAF3 and Rab proteins.
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spelling pubmed-59866282018-06-05 Rab1a rescues the toxicity of PRAF3 Oshikane, Hiroyuki Watabe, Masahiko Kikuchi-Utsumi, Kazue Nakaki, Toshio Biochem Biophys Rep Research Article The PRA1-superfamily member PRAF3 plays pivotal roles in membrane traffic as a GDI displacement factor via physical interaction with a variety of Rab proteins, as well as in the modulation of antioxidant glutathione through its interaction with EAAC1 (SLC1A1). Overproduction of PRAF3 is known to be toxic to the host cells, although the factors capable of cancelling the toxicity remained unknown. We here show that Rab1a can rescue the cytotoxicity caused by PRAF3 possibly by “positively” regulating ER-Golgi trafficking, cancelling the “negative” modulation by PRAF3. Our results illuminate the close physiological relationship between PRAF3 and Rab proteins. Elsevier 2018-03-31 /pmc/articles/PMC5986628/ /pubmed/29872729 http://dx.doi.org/10.1016/j.bbrep.2018.03.002 Text en © 2018 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Oshikane, Hiroyuki
Watabe, Masahiko
Kikuchi-Utsumi, Kazue
Nakaki, Toshio
Rab1a rescues the toxicity of PRAF3
title Rab1a rescues the toxicity of PRAF3
title_full Rab1a rescues the toxicity of PRAF3
title_fullStr Rab1a rescues the toxicity of PRAF3
title_full_unstemmed Rab1a rescues the toxicity of PRAF3
title_short Rab1a rescues the toxicity of PRAF3
title_sort rab1a rescues the toxicity of praf3
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5986628/
https://www.ncbi.nlm.nih.gov/pubmed/29872729
http://dx.doi.org/10.1016/j.bbrep.2018.03.002
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AT kikuchiutsumikazue rab1arescuesthetoxicityofpraf3
AT nakakitoshio rab1arescuesthetoxicityofpraf3

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