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• W2555322488 startingPage "464" @default.
• W2555322488 abstract "Abstract Giardia lamblia is a unicellular organism, showing a polarity with two nuclei and cytoskeletal structures. Accurate positioning of these organelles is essential for division of G. lamblia , which is poorly understood. Giardia lamblia end‐binding 1 (Gl EB 1) protein and G. lamblia aurora kinase (Gl AK ) have been shown to modulate microtubule ( MT ) distribution during cytokinesis. A direct association between Gl EB 1 and Gl AK was demonstrated. Like Gl EB 1, Gl AK was also found at nuclear envelopes and median bodies of G. lamblia . In vitro kinase assays using Giardia lysates immunoprecipitated with anti‐Gl AK antibodies or recombinant Gl AK suggested that Gl EB 1 is a substrate of Gl AK . Site‐directed mutagenesis indicated that threonine‐205 in Gl AK was auto‐phosphorylated and that Gl AK phosphorylated serine (Ser)‐148 in Gl EB 1. Ectopic expression of a mutant Gl EB 1 (with conversion of Ser‐148 into alanine of Gl EB 1) resulted in an increased number of Giardia cells with division defects. Treatment of G. lamblia with an AK inhibitor triggered cytokinesis defects, and ectopic expression of a phospho‐mimetic mutant Gl EB 1 (with conversion of Ser‐148 into aspartate) rescued the defects in Giardia cell division caused by the AK inhibitor. These results suggested that phosphorylation of Gl EB 1 played a role in cytokinesis in G. lamblia ." @default.
• W2555322488 created "2016-11-30" @default.
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• W2555322488 date "2016-12-14" @default.
• W2555322488 modified "2023-10-04" @default.
• W2555322488 title "Phosphorylation of Serine 148 in <i>Giardia lamblia</i> End-binding 1 Protein is Important for Cell Division" @default.
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• W2555322488 doi "https://doi.org/10.1111/jeu.12384" @default.
• W2555322488 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27859890" @default.
• W2555322488 hasPublicationYear "2016" @default.
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