Ismael, A and Tian, W and Waszczak, N and Wang, X and Cao, Y and Suchkov, D and Bar, E and Metodiev, M and Liang, J and Arkowitz, RA and Stone, DE (2016) Gβ promotes pheromone receptor polarization and yeast chemotropism by inhibiting receptor phosphorylation. Science Signaling, 9 (423). ra38-. DOI https://doi.org/10.1126/scisignal.aad4376
Ismael, A and Tian, W and Waszczak, N and Wang, X and Cao, Y and Suchkov, D and Bar, E and Metodiev, M and Liang, J and Arkowitz, RA and Stone, DE (2016) Gβ promotes pheromone receptor polarization and yeast chemotropism by inhibiting receptor phosphorylation. Science Signaling, 9 (423). ra38-. DOI https://doi.org/10.1126/scisignal.aad4376
Ismael, A and Tian, W and Waszczak, N and Wang, X and Cao, Y and Suchkov, D and Bar, E and Metodiev, M and Liang, J and Arkowitz, RA and Stone, DE (2016) Gβ promotes pheromone receptor polarization and yeast chemotropism by inhibiting receptor phosphorylation. Science Signaling, 9 (423). ra38-. DOI https://doi.org/10.1126/scisignal.aad4376
Abstract
Gradient-directed cell migration (chemotaxis) and growth (chemotropism) are processes that are essential to the development and life cycles of all species. Cells use surface receptors to sense the shallow chemical gradients that elicit chemotaxis and chemotropism. Slight asymmetries in receptor activation are amplified by downstream signaling systems, which ultimately induce dynamic reorganization of the cytoskeleton. During the mating response of budding yeast, a model chemotropic system, the pheromone receptors on the plasma membrane polarize to the side of the cell closest to the stimulus. Although receptor polarization occurs before and independently of actin cable-dependent delivery of vesicles to the plasma membrane (directed secretion), it requires receptor internalization. Phosphorylation of pheromone receptors by yeast casein kinase 1 or 2 (Yck1/2) stimulates their internalization. We showed that the pheromone-responsive G?? dimer promotes the polarization of the pheromone receptor by interacting with Yck1/2 and locally inhibiting receptor phosphorylation. We also found that receptor phosphorylation is essential for chemotropism, independently of its role in inducing receptor internalization. A mathematical model supports the idea that the interaction between G?? and Yck1/2 results in differential phosphorylation and internalization of the pheromone receptor and accounts for its polarization before the initiation of directed secretion.
Item Type: | Article |
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Uncontrolled Keywords: | Cell Membrane; Saccharomyces cerevisiae; Casein Kinase I; Adaptor Proteins, Signal Transducing; GTPase-Activating Proteins; GTP-Binding Protein beta Subunits; GTP-Binding Protein gamma Subunits; Saccharomyces cerevisiae Proteins; Luminescent Proteins; Receptors, Pheromone; Pheromones; Microscopy, Confocal; Signal Transduction; Chemotaxis; Cell Polarity; Protein Binding; Phosphorylation; Algorithms; Models, Biological; Computer Simulation; Receptors, Mating Factor; Protein Multimerization; Time-Lapse Imaging |
Subjects: | Q Science > QH Natural history > QH301 Biology |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 25 May 2016 09:39 |
Last Modified: | 24 May 2024 11:08 |
URI: | http://repository.essex.ac.uk/id/eprint/16649 |
Available files
Filename: Ismael_et_al_Sci_Signal_accepted_manuscript.pdf
Filename: Ismael_et_al_SI_9_ra38_SM.pdf