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 AbstractEmission of volatile organic compounds from composting of different solid wastes: abatement by biofiltration    Next Abstract"Do flower color and floral scent of silene species affect host preference of Hadena bicruris, a seed-eating pollinator, under field conditions?" »

J Cell Biol


Title:Localization of the Kar3 kinesin heavy chain-related protein requires the Cik1 interacting protein
Author(s):Page BD; Satterwhite LL; Rose MD; Snyder M;
Address:"Department of Biology, Yale University, New Haven, Connecticut 06520"
Journal Title:J Cell Biol
Year:1994
Volume:124
Issue:4
Page Number:507 - 519
DOI: 10.1083/jcb.124.4.507
ISSN/ISBN:0021-9525 (Print) 1540-8140 (Electronic) 0021-9525 (Linking)
Abstract:"The Kar3 protein (Kar3p), a protein related to kinesin heavy chain, and the Cik1 protein (Cik1p) appear to participate in the same cellular processes in S. cerevisiae. Phenotypic analysis of mutants indicates that both CIK1 and KAR3 participate in spindle formation and karyogamy. In addition, the expression of both genes is induced by pheromone treatment. In vegetatively growing cells, both Cik1::beta-gal and Kar3::beta-gal fusions localize to the spindle pole body (SPB), and after pheromone treatment both fusion proteins localize to the spindle pole body and cytoplasmic microtubules. The dependence of Cik1p and Kar3p localization upon one another was investigated by indirect immunofluorescence of fusion proteins in pheromone-treated cells. The Cik1p::beta-gal fusion does not localize to the SPB or microtubules in a kar3 delta strain, and the Kar3p::beta-gal fusion protein does not localize to microtubule-associated structures in a cik1 delta strain. Thus, these proteins appear to be interdependent for localization to the SPB and microtubules. Analysis by both the two-hybrid system and co-immunoprecipitation experiments indicates that Cik1p and kar3p interact, suggesting that they are part of the same protein complex. These data indicate that interaction between a putative kinesin heavy chain-related protein and another protein can determine the localization of motor activity and thereby affect the functional specificity of the motor complex"
Keywords:Cytoplasm/metabolism Fluorescent Antibody Technique Fungal Proteins/genetics/*metabolism Immunohistochemistry Karyotyping *Microtubule Proteins *Microtubule-Associated Proteins Microtubules/metabolism Phenotype Pheromones Precipitin Tests Saccharomyces ce;
Notes:"MedlinePage, B D Satterwhite, L L Rose, M D Snyder, M eng R01 GM037739/GM/NIGMS NIH HHS/ GM36494/GM/NIGMS NIH HHS/ GM37739/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1994/02/01 J Cell Biol. 1994 Feb; 124(4):507-19. doi: 10.1083/jcb.124.4.507"

 
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 26-12-2024