Interacting Protein Kinases Involved in the Regulation of Flagellar Length
| Autor: | Christel Schmetz, Maja Erdmann, Anne Scholz, Martin Wiese, Inga M. Melzer |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Leishmania mexicana
Molecular Sequence Data Protozoan Proteins Mitogen-activated protein kinase kinase Flagellum RS Animals Amino Acid Sequence Phosphorylation Amastigote Molecular Biology Mitogen-Activated Protein Kinase Kinases biology Kinase Articles Cell Biology biology.organism_classification Leishmania Recombinant Proteins Cell biology Enzyme Activation Phenotype Flagella Mitogen-activated protein kinase Mutation biology.protein Sequence Alignment Gene Deletion |
| Zdroj: | Molecular Biology of the Cell. 17:2035-2045 |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e05-10-0976 |
| Popis: | A striking difference of the life stages of the protozoan parasite Leishmania is a long flagellum in the insect stage promastigotes and a rudimentary organelle in the mammalian amastigotes. LmxMKK, a mitogen-activated protein (MAP) kinase kinase from Leishmania mexicana, is required for growth of a full-length flagellum. We identified LmxMPK3, a MAP kinase homologue, with a similar expression pattern as LmxMKK being not detectable in amastigotes, up-regulated during the differentiation to promastigotes, constantly expressed in promastigotes, and shut down during the differentiation to amastigotes. LmxMPK3 null mutants resemble the LmxMKK knockouts with flagella reduced to one-fifth of the wild-type length, stumpy cell bodies, and vesicles and membrane fragments in the flagellar pocket. A constitutively activated recombinant LmxMKK activates LmxMPK3 in vitro. Moreover, LmxMKK is likely to be directly involved in the phosphorylation of LmxMPK3 in vivo. Finally, LmxMPK3 is able to phosphorylate LmxMKK, indicating a possible feedback regulation. This is the first time that two interacting components of a signaling cascade have been described in the genus Leishmania. Moreover, we set the stage for the analysis of reversible phosphorylation in flagellar morphogenesis. |
| Databáze: | OpenAIRE |
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