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 AbstractSources of Controversy Surrounding Latitudinal Patterns in Herbivory and Defense    Next AbstractThe prepared mind of the worm »

Mol Biol Cell


Title:"The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution"
Author(s):Antebi A; Fink GR;
Address:"Whitehead Institute of Biomedical Research, Cambridge, Massachusetts"
Journal Title:Mol Biol Cell
Year:1992
Volume:3
Issue:6
Page Number:633 - 654
DOI: 10.1091/mbc.3.6.633
ISSN/ISBN:1059-1524 (Print) 1059-1524 (Linking)
Abstract:"PMR1, a Ca(2+)-adenosine triphosphatase (ATPase) homologue in the yeast Saccharomyces cerevisiae localizes to a novel Golgi-like organelle. Consistent with a Golgi localization, the bulk of PMR1 comigrates with Golgi markers in subcellular fractionation experiments, and staining of PMR1 by indirect immunofluorescence reveals a punctate pattern resembling Golgi staining in yeast. However, PMR1 shows only partial colocalization with known Golgi markers, KEX2 and SEC7, in double-label immunofluorescence experiments. The effect of PMR1 on Golgi function is indicated by pleiotropic defects in various Golgi processes in pmr1 mutants, including impaired proteolytic processing of pro-alpha factor and incomplete outer chain glycosylation of invertase. Consistent with the proposed role of PMR1 as a Ca2+ pump, these defects are reversed by the addition of millimolar levels of extracellular Ca2+, suggesting that Ca2+ disposition is essential to normal Golgi function. Absence of PMR1 function partially suppresses the temperature-sensitive growth defects of several sec mutants, and overexpression of PMR1 restricts the growth of others. Some of these interactions are modulated by changes in external Ca2+ concentrations. These results imply a global role for Ca2+ in the proper function of components governing transit and processing through the secretory pathway"
Keywords:"Amino Acid Sequence Base Sequence Biological Transport/physiology Calcium-Transporting ATPases/analysis/*physiology Carboxypeptidases/analysis Cathepsin A Epitopes Fungal Proteins/analysis/*metabolism Genes, Fungal/physiology Glycosylation Golgi Apparatus;"
Notes:"MedlineAntebi, A Fink, G R eng GM-35010/GM/NIGMS NIH HHS/ GM-40266/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 1992/06/01 Mol Biol Cell. 1992 Jun; 3(6):633-54. doi: 10.1091/mbc.3.6.633"

 
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 16-11-2024