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A more recent version of this article appeared on December 1, 2002
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Submitted on July 9, 2002
Revised on August 12, 2002
Accepted on August 21, 2002
1 Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599; and Graduate Program in Cell and Molecular Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599
2 Department of Biology, Fort Lewis College, Durango, CO 81301
3 Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599; and Cystic Fibrosis/Pulmonary Research and Treatment Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599
* Corresponding author. E-mail address: milg{at}med.unc.edu.
Although protein kinase A (PKA) activation is known to increase ciliary beat frequency (CBF) in humans the molecular mechanisms involved are unknown. We demonstrate that PKA is associated with ciliary axonemes where it specifically phosphorylates a 23 kD protein. Because PKA is often localized to subcellular compartments in close proximity to its substrate(s) via interactions with A-kinase anchoring proteins (AKAPs), we investigated whether an AKAP was also associated with ciliary axonemes. These studies have identified a novel AKAP that is highly enriched in airway axonemes. The mRNA for this 28 kD AKAP (AKAP28) is upregulated 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 CBF.
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