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 AbstractIdentification and initial characterization of an autocrine pheromone receptor in the protozoan ciliate Euplotes raikovi    Next AbstractDetermining larval host plant use by a polyphagous lepidopteran through analysis of adult moths for plant secondary metabolites »

Mol Biol Cell


Title:The autocrine mitogenic loop of the ciliate Euplotes raikovi: the pheromone membrane-bound forms are the cell binding sites and potential signaling receptors of soluble pheromones
Author(s):Ortenzi C; Alimenti C; Vallesi A; Di Pretoro B; Terza AL; Luporini P;
Address:"Dipartimento di Biologia Molecolare Cellulare Animale, University of Camerino, 62032 Camerino (MC), Italy"
Journal Title:Mol Biol Cell
Year:2000
Volume:11
Issue:4
Page Number:1445 - 1455
DOI: 10.1091/mbc.11.4.1445
ISSN/ISBN:1059-1524 (Print) 1059-1524 (Linking)
Abstract:"Homologous proteins, denoted pheromones, promote cell mitotic proliferation and mating pair formation in the ciliate Euplotes raikovi, according to whether they bind to cells in an autocrine- or paracrine-like manner. The primary transcripts of the genes encoding these proteins undergo alternate splicing, which generates at least two distinct mRNAs. One is specific for the soluble pheromone, the other for a pheromone isoform that remains anchored to the cell surface as a type II protein, whose extracellular C-terminal region is structurally equivalent to the secreted form. The 15-kDa membrane-bound isoform of pheromone Er-1, denoted Er-1mem and synthesized by the same E. raikovi cells that secrete Er-1, has been purified from cell membranes by affinity chromatography prepared with matrix-bound Er-1, and its extracellular and cytoplasmic regions have been expressed as recombinant proteins. Using the purified material and these recombinant proteins, it has been shown that Er-1mem has the property of binding pheromones competitively through its extracellular pheromone-like domain and associating reversibly and specifically with a guanine nucleotide-binding protein through its intracellular domain. It has been concluded that the membrane-bound pheromone isoforms of E. raikovi represent the cell effective pheromone binding sites and are functionally equipped for transducing the signal generated by this binding"
Keywords:"Amino Acid Sequence Animals Autocrine Communication/*physiology Chromatography, Affinity Euplotes/chemistry/*physiology Membrane Proteins/chemistry/isolation & purification/*metabolism Models, Molecular Molecular Sequence Data Molecular Weight Pheromones/;"
Notes:"MedlineOrtenzi, C Alimenti, C Vallesi, A Di Pretoro, B Terza, A L Luporini, P eng Research Support, Non-U.S. Gov't 2000/04/06 Mol Biol Cell. 2000 Apr; 11(4):1445-55. doi: 10.1091/mbc.11.4.1445"

 
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