Journal
JOURNAL OF CELL BIOLOGY
Volume 184, Issue 5, Pages 721-736Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200804154
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Funding
- Medical Research Council for an Infrastructure Award
- Joint Research Equipment Initiative Grant to establish the School of Medical Sciences Cell Imaging Facility
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CD317/tetherin is a lipid raft-associated integral membrane protein with a novel topology. It has a short N-terminal cytosolic domain, a conventional transmembrane domain, and a C-terminal glycosylphosphatidylinositol anchor. We now show that CD317 is expressed at the apical surface of polarized epithelial cells, where it interacts indirectly with the underlying actin cytoskeleton. CD317 is linked to the apical actin network via the proteins RICH2, EBP50, and ezrin. Knocking down expression of either CD317 or RICH2 gives rise to the same phenotype: a loss of the apical actin network with concomitant loss of apical microvilli, an increase in actin bundles at the basal surface, and a reduction in cell height without any loss of tight junctions, transepithelial resistance, or the polarized targeting of apical and basolateral membrane proteins. Thus, CD317 provides a physical link between lipid rafts and the apical actin network in polarized epithelial cells and is crucial for the maintenance of microvilli in such cells.
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