Your browser doesn't support javascript.
loading
Dynamin-SNARE interactions control trans-SNARE formation in intracellular membrane fusion.
Alpadi, Kannan; Kulkarni, Aditya; Namjoshi, Sarita; Srinivasan, Sankaranarayanan; Sippel, Katherine H; Ayscough, Kathryn; Zieger, Martin; Schmidt, Andrea; Mayer, Andreas; Evangelista, Michael; Quiocho, Florante A; Peters, Christopher.
Afiliação
  • Alpadi K; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.
Nat Commun ; 4: 1704, 2013.
Article em En | MEDLINE | ID: mdl-23591871
The fundamental processes of membrane fission and fusion determine size and copy numbers of intracellular organelles. Although SNARE proteins and tethering complexes mediate intracellular membrane fusion, fission requires the presence of dynamin or dynamin-related proteins. Here we study these reactions in native yeast vacuoles and find that the yeast dynamin homologue Vps1 is not only an essential part of the fission machinery, but also controls membrane fusion by generating an active Qa SNARE-tethering complex pool, which is essential for trans-SNARE formation. Our findings provide new insight into the role of dynamins in membrane fusion by directly acting on SNARE proteins.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Dinaminas / Proteínas SNARE / Fusão de Membrana Idioma: En Revista: Nat Commun Assunto da revista: BIOLOGIA / CIENCIA Ano de publicação: 2013 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Dinaminas / Proteínas SNARE / Fusão de Membrana Idioma: En Revista: Nat Commun Assunto da revista: BIOLOGIA / CIENCIA Ano de publicação: 2013 Tipo de documento: Article País de afiliação: Estados Unidos