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• W2159900734 abstract "Cilia and flagella are cell organelles that are highly conserved throughout evolution. For many years, the green biflagellate alga Chlamydomonas reinhardtii has served as a model for examination of the structure and function of its flagella, which are similar to certain mammalian cilia. Proteome analysis revealed the presence of several kinases and protein phosphatases in these organelles. Reversible protein phosphorylation can control ciliary beating, motility, signaling, length, and assembly. Despite the importance of this posttranslational modification, the identities of many ciliary phosphoproteins and knowledge about their in vivo phosphorylation sites are still missing. Here we used immobilized metal affinity chromatography to enrich phosphopeptides from purified flagella and analyzed them by mass spectrometry. One hundred forty-one phosphorylated peptides were identified, belonging to 32 flagellar proteins. Thereby, 126 in vivo phosphorylation sites were determined. The flagellar phosphoproteome includes different structural and motor proteins, kinases, proteins with protein interaction domains, and many proteins whose functions are still unknown. In several cases, a dynamic phosphorylation pattern and clustering of phosphorylation sites were found, indicating a complex physiological status and specific control by reversible protein phosphorylation in the flagellum." @default.
• W2159900734 created "2016-06-24" @default.
• W2159900734 creator A5022468377 @default.
• W2159900734 creator A5023567333 @default.
• W2159900734 creator A5062610781 @default.
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• W2159900734 date "2009-07-01" @default.
• W2159900734 modified "2023-10-03" @default.
• W2159900734 title "Analysis of Flagellar Phosphoproteins from <i>Chlamydomonas reinhardtii</i>" @default.
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• W2159900734 doi "https://doi.org/10.1128/ec.00067-09" @default.
• W2159900734 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2708455" @default.
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• W2159900734 hasPublicationYear "2009" @default.
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