ThePXL1Gene ofSaccharomyces cerevisiaeEncodes a Paxillin-like Protein Functioning in Polarized Cell Growth
| Autor: | Nancy A. Mackin, Tarek J. Sousou, Scott E. Erdman |
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| Rok vydání: | 2004 |
| Předmět: |
Scaffold protein
Saccharomyces cerevisiae Proteins Genotype Cell Survival Green Fluorescent Proteins Molecular Sequence Data Saccharomyces cerevisiae Plasma protein binding Biology Open Reading Frames Amino Acid Sequence Cytoskeleton Molecular Biology Peptide sequence Actin Paxillin Adaptor Proteins Signal Transducing Sequence Homology Amino Acid Temperature Articles Cell Biology Phosphoproteins biology.organism_classification Actins Protein Structure Tertiary Cell biology Cytoskeletal Proteins Luminescent Proteins Open reading frame Phenotype Microscopy Fluorescence biology.protein Genome Fungal Carrier Proteins Cell Division Plasmids Protein Binding Signal Transduction |
| Zdroj: | Molecular Biology of the Cell. 15:1904-1917 |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | The Saccharomyces cerevisiae open reading frame YKR090w encodes a predicted protein displaying similarity in organization to paxillin, a scaffolding protein that organizes signaling and actin cytoskeletal regulating activities in many higher eucaryotic cell types. We found that YKR090w functions in a manner analogous to paxillin as a mediator of polarized cell growth; thus, we have named this gene PXL1 (Paxillin-like protein 1). Analyses of pxl1Δ strains show that PXL1 is required for the selection and maintenance of polarized growth sites during vegetative growth and mating. Genetic analyses of strains lacking both PXL1 and the Rho GAP BEM2 demonstrate that such cells display pronounced growth defects in response to different conditions causing Rho1 pathway activation. PXL1 also displays genetic interactions with the Rho1 effector FKS1. Pxl1p may therefore function as a modulator of Rho-GTPase signaling. A GFP::Pxl1 fusion protein localizes to sites of polarized cell growth. Experiments mapping the localization determinants of Pxl1p demonstrate the existence of localization mechanisms conserved between paxillin and Pxl1p and indicate an evolutionarily ancient and conserved role for LIM domain proteins in acting to modulate cell signaling and cytoskeletal organization during polarized growth. |
| Databáze: | OpenAIRE |
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