Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Rtn1p is involved in structuring the cortical endoplasmic reticulum

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • De Craene, J. O.
  • Coleman, J.
  • de Martin, P. E.
  • Pypaert, M.
  • Anderson, S.
  • Yates III, John
  • Ferro-Novick, S.
  • Novick, P.

publication date

  • July 2006

journal

  • Molecular Biology of the Cell  Journal

abstract

  • The endoplasmic reticulum (ER) contains both cisternal and reticular elements in one contiguous structure. We identified rtn1Delta in a systematic screen for yeast mutants with altered ER morphology. The ER in rtn1Delta cells is predominantly cisternal rather than reticular, yet the net surface area of ER is not significantly changed. Rtn1-green fluorescent protein (GFP) associates with the reticular ER at the cell cortex and with the tubules that connect the cortical ER to the nuclear envelope, but not with the nuclear envelope itself. Rtn1p overexpression also results in an altered ER structure. Rtn proteins are found on the ER in a wide range of eukaryotes and are defined by two membrane-spanning domains flanking a conserved hydrophilic loop. Our results suggest that Rtn proteins may direct the formation of reticulated ER. We independently identified Rtn1p in a proteomic screen for proteins associated with the exocyst vesicle tethering complex. The conserved hydophilic loop of Rtn1p binds to the exocyst subunit Sec6p. Overexpression of this loop results in a modest accumulation of secretory vesicles, suggesting impaired exocyst function. The interaction of Rtn1p with the exocyst at the bud tip may trigger the formation of a cortical ER network in yeast buds.

subject areas

  • Endoplasmic Reticulum
  • Gene Deletion
  • Intracellular Membranes
  • Membrane Proteins
  • Membrane Transport Proteins
  • Organelles
  • Proteomics
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Secretory Vesicles
scroll to property group menus

Identity

PubMed Central ID

  • PMC1483037

International Standard Serial Number (ISSN)

  • 1059-1524

Digital Object Identifier (DOI)

  • 10.1091/mbc.E06-01-0080

PubMed ID

  • 16624861
scroll to property group menus

Additional Document Info

start page

  • 3009

end page

  • 3020

volume

  • 17

issue

  • 7

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support