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Developmentally regulated GTP-binding protein 2 is required for stabilization of Rac1-positive membrane tubules.
Mani, Muralidharan; Lee, Unn Hwa; Yoon, Nal Ae; Yoon, Eun Hye; Lee, Byung Ju; Cho, Wha Ja; Park, Jeong Woo.
Afiliação
  • Mani M; Department of Biological Sciences, University of Ulsan, Ulsan 680-749, South Korea.
  • Lee UH; Department of Biological Sciences, University of Ulsan, Ulsan 680-749, South Korea.
  • Yoon NA; Department of Biological Sciences, University of Ulsan, Ulsan 680-749, South Korea.
  • Yoon EH; Department of Biological Sciences, University of Ulsan, Ulsan 680-749, South Korea.
  • Lee BJ; Department of Biological Sciences, University of Ulsan, Ulsan 680-749, South Korea.
  • Cho WJ; Metainflammation Research Center, University of Ulsan, Ulsan 680-749, South Korea.
  • Park JW; Department of Biological Sciences, University of Ulsan, Ulsan 680-749, South Korea. Electronic address: jwpark@ulsan.ac.kr.
Biochem Biophys Res Commun ; 493(1): 758-764, 2017 11 04.
Article em En | MEDLINE | ID: mdl-28865956
ABSTRACT
Previously we have reported that developmentally regulated GTP-binding protein 2 (DRG2) localizes on Rab5 endosomes and plays an important role in transferrin (Tfn) recycling. We here identified DRG2 as a key regulator of membrane tubule stability. At 30 min after Tfn treatment, DRG2 localized to membrane tubules which were enriched with phosphatidylinositol 4-monophosphate [PI(4)P] and did not contain Rab5. DRG2 interacted with Rac1 more strongly with GTP-bound Rac1 and tubular localization of DRG2 depended on Rac1 activity. DRG2 depletion led to destabilization of membrane tubules, while ectopic expression of DRG2 rescued the stability of the membrane tubules in DRG2-depleted cells. Our results reveal a novel mechanism for regulation of membrane tubule stability mediated by DRG2.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fosfolipídeos / Endossomos / Neuropeptídeos / Membrana Celular / Proteínas de Ligação ao GTP / Proteínas rac1 de Ligação ao GTP Limite: Animals / Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fosfolipídeos / Endossomos / Neuropeptídeos / Membrana Celular / Proteínas de Ligação ao GTP / Proteínas rac1 de Ligação ao GTP Limite: Animals / Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article