A Dynamin Homolog Promotes the Transition from Hemifusion to Content Mixing in Intracellular Membrane Fusion. (25th February 2014)

• Record Type: Journal Article
• Authors: Kulkarni, Aditya; Alpadi, Kannan; Sirupangi, Tirupataiah; Peters, Christopher
• Is Part Of: Traffic. Volume 15:Number 5(2014:May)
• Page Start: 558
• Page End: 571
• Publication Date: 2014-02-25
• Subjects: Biological transport -- Periodicals; 571.6
• DOI: 10.1111/tra.12156
• Languages: English
• ISSNs: 1398-9219

Abstract

<abstract abstract-type="graphical" id="tra12156-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p id="tra12156-para-0002">Dynamin family members have been implicated in exocytosis. Vps1 (the yeast dynamin homolog) mutant vacuoles show decreased fusion and <italic>trans</italic>‐Soluble <italic>N</italic>‐ethylmaleimide sensitive factor Attachment Protein Receptor (SNARE) complex formation but comparable hemifusion relative to wild type. Vps1, through its oligomerization and SNARE‐domain binding, brings together multiple t‐SNAREs. This finding uncovers a novel function of Vps1 in coordinating the hemifusion – content mixing transition in yeast vacuole fusion.<boxed-text content-type="graphic" id="tra12156-blkfxd-0001" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg546dx785" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>