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The Saccharomyces cerevisiae RhoGAP Rgd1 is phosphorylated by the Aurora B like kinase Ipl1.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2013 Mar 29; Vol. 433 (1), pp. 1-5. Date of Electronic Publication: 2013 Feb 27. - Publication Year :
- 2013
-
Abstract
- Polarized growth of the yeast Saccharomyces cerevisiae depends on different biological processes and requires several signaling pathways. Signaling is mediated through a set of proteins, which include Rho3p and Rho4p GTPases. Although these two proteins are involved in the control of distinct aspects of polarized growth in yeast, they have a common regulator: the Rgd1 RhoGAP protein. Here we demonstrate that Rgd1p is phosphorylated by the Aurora B like kinase Ipl1 and we observe that loss of Ipl1 function leads to a new Rgd1p distribution in a small part of the cell population.<br /> (Copyright © 2013 Elsevier Inc. All rights reserved.)
- Subjects :
- Aurora Kinases
Cytokinesis
GTPase-Activating Proteins chemistry
GTPase-Activating Proteins genetics
Genes, Fungal
Intracellular Signaling Peptides and Proteins antagonists & inhibitors
Intracellular Signaling Peptides and Proteins genetics
Mutation
Phosphorylation
Protein Processing, Post-Translational
Protein Serine-Threonine Kinases antagonists & inhibitors
Protein Serine-Threonine Kinases genetics
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Saccharomyces cerevisiae cytology
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae growth & development
Saccharomyces cerevisiae Proteins antagonists & inhibitors
Saccharomyces cerevisiae Proteins chemistry
Saccharomyces cerevisiae Proteins genetics
Signal Transduction
GTPase-Activating Proteins metabolism
Intracellular Signaling Peptides and Proteins metabolism
Protein Serine-Threonine Kinases metabolism
Saccharomyces cerevisiae metabolism
Saccharomyces cerevisiae Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 433
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 23454383
- Full Text :
- https://doi.org/10.1016/j.bbrc.2013.02.081