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Vol. 13, Issue 12, 4156-4166, December 2002

Characterization of an A-Kinase Anchoring Protein in Human Ciliary Axonemes

Patricia L. Kultgen,^* Sherell K. Byrd, Lawrence E. Ostrowski,^*§ and Sharon L. Milgram^*§

 ^*Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599;  Graduate Program in Cell and Molecular Physiology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599;  Department of Biology, Fort Lewis College, Durango, Colorado 81301; and  ^§Cystic Fibrosis/Pulmonary Research and Treatment Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599

Although protein kinase A (PKA) activation is known to increase ciliary beat frequency in humans the molecular mechanisms involved are unknown. We demonstrate that PKA is associated with ciliary axonemes where it specifically phosphorylates a 23-kDa protein. Because PKA is often localized to subcellular compartments in proximity to its substrate(s) via interactions with A-kinase-anchoring proteins (AKAPs), we investigated whether an AKAP was also associated with ciliary axonemes. This study has identified a novel 28 kDa AKAP (AKAP28)that is highly enriched in airway axonemes. The mRNA for AKAP28 is up-regulated as primary airway cells differentiate and is specifically expressed in tissues containing cilia and/or flagella. Additionally, both Western blot and immunostaining data show that AKAP28 is enriched in airway cilia. These data demonstrate that we have identified the first human axonemal AKAP, a protein that likely plays a role in the signaling necessary for efficient modulation of ciliary beat frequency.

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Corresponding author. E-mail address: milg{at}med.unc.edu.

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Molecular Biology of the Cell
Vol. 13, 4156-4166, December 2002
Copyright © 2002 by The American Society for Cell Biology

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