A conserved CaM- and radial spoke associated complex mediates regulation of flagellar dynein activity.

A conserved CaM- and radial spoke associated complex mediates regulation of flagellar dynein activity.
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DOI:
10.1083/jcb.200703107
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发表时间:
2007-11-05
影响因子:
7.8
通讯作者:
Smith, Elizabeth F.
Smith, Elizabeth F.
中科院分区:
生物学1区
文献类型:
--
作者:
Dymek, Erin E.;Smith, Elizabeth F.

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For virtually all cilia and eukaryotic flagella, the second messengers calcium and cyclic adenosine monophosphate are implicated in modulating dynein- driven microtubule sliding to regulate beating. Calmodulin (CaM) localizes to the axoneme and is a key calcium sensor involved in regulating motility. Using immunoprecipitation and mass spectrometry, we identify members of a CaM-containing complex that are involved in regulating dynein activity. This complex includes flagellar-associated protein 91 (FAP91), which shares considerable sequence similarity to AAT-1, a protein originally identified in testis as an A-kinase anchor protein (AKAP)– binding protein. FAP91 directly interacts with radial spoke protein 3 (an AKAP), which is located at the base of the spoke. In a microtubule sliding assay, the addition of antibodies generated against FAP91 to mutant axonemes with reduced dynein activity restores dynein activity to wild-type levels. These combined results indicate that the CaM- and spoke-associated complex mediates regulatory signals between the radial spokes and dynein arms.
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