Dynamin−SNARE interactions control trans-SNARE formation in intracellular membrane fusion

Kannan Alpadi, Aditya Kulkarni, Sarita Namjoshi, Sankaranarayanan Srinivasan, Katherine H. Sippel, Kathryn Ayscough, Martin Zieger, Andrea Schmidt, Andreas Mayer, Michael Evangelista, Florante A. Quiocho and Christopher Peters ()
Additional contact information
Kannan Alpadi: Baylor College of Medicine
Aditya Kulkarni: Baylor College of Medicine
Sarita Namjoshi: Baylor College of Medicine
Sankaranarayanan Srinivasan: Baylor College of Medicine
Katherine H. Sippel: Baylor College of Medicine
Kathryn Ayscough: University of Sheffield, Western Bank
Martin Zieger: Université de Lausanne
Andrea Schmidt: Université de Lausanne
Andreas Mayer: Université de Lausanne
Michael Evangelista: Baylor College of Medicine
Florante A. Quiocho: Baylor College of Medicine
Christopher Peters: Baylor College of Medicine

Nature Communications, 2013, vol. 4, issue 1, 1-8

Abstract: Abstract 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.

Date: 2013
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms2724 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2724

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms2724

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().