tsunami, the Dictyostelium homolog of the Fused kinase, is required for polarization and chemotaxis
| Autor: | Jonathan Franca-Koh, Yuan Xiong, Pablo A. Iglesias, Ross M. Bickford, David A. Knecht, Peter N. Devreotes, Yu Long, Mei Yu Chen, Linnan Tang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Molecular Sequence Data
Phosphatidylinositols Microtubules Dictyostelium discoideum Microtubule Cell Movement Genetics Cyclic AMP Animals Drosophila Proteins Dictyostelium Amino Acid Sequence Kinase activity Sequence Deletion biology Sequence Homology Amino Acid Chemotaxis Gene Expression Profiling Cell Polarity Cell Differentiation biology.organism_classification Actins Cell biology Protein Transport Phenotype Protein kinase domain Biochemistry Mutation Pseudopodia Signal transduction Developmental Biology Research Paper Signal Transduction Subcellular Fractions |
| Popis: | In a forward genetic screen for chemotaxis mutants in Dictyostelium discoideum, we identified a loss-of-function mutation, designated tsunami, encoding a homolog of the Fused kinase. Cells lacking tsuA function could not effectively perform chemotaxis and were unable to become polarized or correctly orient pseudopods in chemotactic gradients. While tsuA− cells were able to couple receptor occupancy to phosphatidylinositol (3,4,5) trisphosphate (PIP3) production and actin polymerization, the PIP3 response was prolonged and basal F-actin levels were increased. Interestingly, TsuA localizes to the microtubule network and puncta mainly found at the cell periphery. Analysis of the gene uncovered a novel C-terminal domain that we designated the Tsunami Homology (TH) domain. Both the kinase domain and the TH domain are required to rescue the phenotypic defects of tsuA− cells. While kinase activity is not required for localization to microtubules, the TH domain is essential. Thus, localization of kinase activity to microtubules is critical for TsuA function. We propose that functions in association with the microtubule network may underlie the divergent roles of Fused kinase proteins in different organisms. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|