Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractProteomic analysis of Daphnia magna hints at molecular pathways involved in defensive plastic responses    Next AbstractPhenotypic plasticity of mate recognition systems prevents sexual interference between two sympatric leaf beetle species »

Nat Cell Biol


Title:Sorting signals can direct receptor-mediated export of soluble proteins into COPII vesicles
Author(s):Otte S; Barlowe C;
Address:"Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA"
Journal Title:Nat Cell Biol
Year:2004
Volume:20041031
Issue:12
Page Number:1189 - 1194
DOI: 10.1038/ncb1195
ISSN/ISBN:1465-7392 (Print) 1465-7392 (Linking)
Abstract:"Soluble secretory proteins are first translocated across endoplasmic reticulum (ER) membranes and folded in a specialized ER luminal environment. Fully folded and assembled secretory cargo are then segregated from ER-resident proteins into COPII-derived vesicles or tubular elements for anterograde transport. Mechanisms of bulk-flow, ER-retention and receptor-mediated export have been suggested to operate during this transport step, although these mechanisms are poorly understood. In yeast, there is evidence to suggest that Erv29p functions as a transmembrane receptor for the export of certain soluble cargo proteins including glycopro-alpha-factor (gpalphaf), the precursor of alpha-factor mating pheromone. Here we identify a hydrophobic signal within the pro-region of gpalphaf that is necessary for efficient packaging into COPII vesicles and for binding to Erv29p. When fused to Kar2p, an ER-resident protein, the pro-region sorting signal was sufficient to direct Erv29p-dependent export of the fusion protein into COPII vesicles. These findings indicate that specific motifs within soluble secretory proteins function in receptor-mediated export from the ER. Moreover, positive sorting signals seem to predominate over potential ER-retention mechanisms that may operate in localizing ER-resident proteins such as Kar2p"
Keywords:COP-Coated Vesicles/*metabolism Endoplasmic Reticulum/*metabolism Fungal Proteins/metabolism HSP70 Heat-Shock Proteins/metabolism Mating Factor Membrane Proteins/metabolism Peptides/metabolism Protein Binding/physiology Protein Precursors/metabolism Prote;
Notes:"MedlineOtte, Stefan Barlowe, Charles eng Research Support, U.S. Gov't, P.H.S. England 2004/11/02 Nat Cell Biol. 2004 Dec; 6(12):1189-94. doi: 10.1038/ncb1195. Epub 2004 Oct 31"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 17-11-2024