Affordable Access

deepdyve-link
Publisher Website

The cell polarity proteins Boi1p and Boi2p stimulate vesicle fusion at the plasma membrane of yeast cells.

Authors
  • Kustermann, Jochen1
  • Wu, Yehui1
  • Rieger, Lucia1
  • Dedden, Dirk1
  • Phan, Tamara1
  • Walther, Paul2
  • Dünkler, Alexander1
  • Johnsson, Nils
  • 1 Institute of Molecular Genetics and Cell Biology, Department of Biology, Ulm University, James-Franck-Ring N27, D-89081 Ulm, Germany. , (Germany)
  • 2 Central Facility for Electron Microscopy, Ulm University, Albert-Einstein-Allee 11, D-89069 Ulm, Germany. , (Germany)
Type
Published Article
Journal
Journal of Cell Science
Publisher
The Company of Biologists
Publication Date
Sep 15, 2017
Volume
130
Issue
18
Pages
2996–3008
Identifiers
DOI: 10.1242/jcs.206334
PMID: 28751498
Source
Medline
Keywords
License
Unknown

Abstract

Eukaryotic cells can direct secretion to defined regions of their plasma membrane. These regions are distinguished by an elaborate architecture of proteins and lipids that are specialized to capture and fuse post-Golgi vesicles. Here, we show that the proteins Boi1p and Boi2p are important elements of this area of active exocytosis at the tip of growing yeast cells. Cells lacking Boi1p and Boi2p accumulate secretory vesicles in their buds. The essential PH domains of Boi1p and Boi2p interact with Sec1p, a protein required for SNARE complex formation and vesicle fusion. Sec1p loses its tip localization in cells depleted of Boi1p and Boi2p but overexpression of Sec1p can partially compensate for their loss. The capacity to simultaneously bind phospholipids, Sec1p, multiple subunits of the exocyst, Cdc42p and the module for generating active Cdc42p identify Boi1p and Boi2p as essential mediators between exocytosis and polar growth.

Report this publication

Statistics

Seen <100 times