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MBC in Press, published online ahead of print November 14, 2007
Mol. Biol. Cell 10.1091/mbc.E07-08-0818

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Submitted on August 23, 2007
Revised on October 29, 2007
Accepted on November 6, 2007

Adducin Promotes Micron-Scale Organization of {beta}2-Spectrin in Lateral Membranes of Bronchial Epithelial Cells

Khadar M. Abdi and Vann Bennett

Howard Hughes Medical Institute and the Department of Cell Biology, Duke University Medical Center, Durham, NC 27710

Monitoring Editor: Ben Margolis

Adducin promotes assembly of spectrin-actin complexes, and is a target for regulation by calmodulin, protein kinase C and rho kinase. We demonstrate here that adducin is required to stabilize preformed lateral membranes of human bronchial epithelial (HBE) cells through interaction with {beta}2-spectrin. We use a Tet-on regulated inducible siRNA system to deplete {alpha}-adducin from confluent HBE cells. Depletion of {alpha}-adducin resulted in increased detergent solubility of spectrin following normal membrane biogenesis during mitosis. Conversely, depletion of {beta}2-spectrin resulted in loss of adducin from the lateral membrane. siRNA-resistant {alpha}-adducin prevented loss of lateral membrane, but only if {alpha}-adducin retained the MARCKS domain that mediates spectrin-actin interactions. Phospho-mimetic versions of adducin with S/D substitutions at PKC phosphorylation sites in the MARCKS domain were not active in rescue. We find that adducin modulates long-range organization of the lateral membrane based on several criteria. First, the lateral membrane of adducin-depleted cells exhibited reduced height, increased curvature, expansion into the basal surface. Moreover, E-cadherin-GFP, which normally is restricted in lateral mobility, rapidly diffuses over distances up to 10 microns. We conclude that adducin acting through spectrin provides a novel mechanism to regulate global properties of the lateral membrane of bronchial epithelial cells.

Address correspondence to: Vann Bennett (v.bennett{at}cellbio.duke.edu)




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