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« Previous AbstractAutocrine mitogenic activity of pheromones produced by the protozoan ciliate Euplotes raikovi    Next Abstract"Characterization of the pheromone gene family of an Antarctic and Arctic protozoan ciliate, Euplotes nobilii" »

Eukaryot Cell


Title:"Autocrine, mitogenic pheromone receptor loop of the ciliate Euplotes raikovi: pheromone-induced receptor internalization"
Author(s):Vallesi A; Ballarini P; Di Pretoro B; Alimenti C; Miceli C; Luporini P;
Address:"Dipartimento di Biologia MCA, Universita di Camerino, 63032 Camerino, Italy"
Journal Title:Eukaryot Cell
Year:2005
Volume:4
Issue:7
Page Number:1221 - 1227
DOI: 10.1128/EC.4.7.1221-1227.2005
ISSN/ISBN:1535-9778 (Print) 1535-9786 (Electronic) 1535-9786 (Linking)
Abstract:"The ciliate Euplotes raikovi produces a family of diffusible signal proteins (pheromones) that function as prototypic growth factors. They may either promote cell growth, by binding to pheromone receptors synthesized by the same cells from which they are secreted (autocrine activity), or induce a temporary cell shift from the growth stage to a mating (sexual) one by binding to pheromone receptors of other, conspecific cells (paracrine activity). In cells constitutively secreting the pheromone Er-1, it was first observed that the expression of the Er-1 receptor 'p15,' a type II membrane protein of 130 amino acids, is quantitatively correlated with the extracellular concentration of secreted pheromone. p15 expression on the cell surface rapidly and markedly increased after the removal of secreted Er-1 and gradually decreased in parallel with new Er-1 secretion. It was then shown that p15 is internalized through endocytic vesicles following Er-1 binding and that the internalization of p15/Er-1 complexes is specifically blocked by the paracrine p15 binding of Er-2, a pheromone structurally homologous to, and thus capable of fully antagonizing, Er-1. Based on previous findings that the p15 pheromone-binding site is structurally equivalent to Er-1 and that Er-1 molecules polymerize in crystals following a pattern of cooperative interaction, it was proposed that p15/Er-1 complexes are internalized as a consequence of their unique property (not shared by p15/Er-2 complexes) of undergoing clustering"
Keywords:"Animals Autocrine Communication/*physiology Euplotes/cytology/*physiology Gene Expression Regulation Membrane Proteins/metabolism Molecular Mimicry/physiology Pheromones/*metabolism Protein Binding/physiology Protein Conformation Protein Structure, Second;"
Notes:"MedlineVallesi, Adriana Ballarini, Patrizia Di Pretoro, Barbara Alimenti, Claudio Miceli, Cristina Luporini, Pierangelo eng Research Support, Non-U.S. Gov't 2005/07/09 Eukaryot Cell. 2005 Jul; 4(7):1221-7. doi: 10.1128/EC.4.7.1221-1227.2005"

 
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Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
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