A
correction
to this article has been published: D'Alterio et al., J. Cell Biol. 171 (6) 1085
Published online 31 October 2005. doi:10.1083/jcb.200507072
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 3, 549-558
Drosophila melanogaster Cad99C, the orthologue of human Usher cadherin PCDH15, regulates the length of microvilli
Cecilia D'Alterio,
Dao D.D. Tran,
Maggie W.Y. Au Yeung,
Michael S.H. Hwang,
Michelle A. Li,
Claudia J. Arana,
Vikram K. Mulligan,
Mary Kubesh,
Praveer Sharma,
Maretta Chase,
Ulrich Tepass, and
Dorothea Godt
Department of Zoology, University of Toronto, Toronto, Ontario, Canada, M5S 3G5
Correspondence to Dorothea Godt: dgodt{at}zoo.utoronto.ca
Actin-based protrusions can form prominent structures on the apical surface of epithelial cells, such as microvilli. Several cytoplasmic factors have been identified that control the dynamics of actin filaments in microvilli. However, it remains unclear whether the plasma membrane participates actively in microvillus formation. In this paper, we analyze the function of Drosophila melanogaster cadherin Cad99C in the microvilli of ovarian follicle cells. Cad99C contributes to eggshell formation and female fertility and is expressed in follicle cells, which produce the eggshells. Cad99C specifically localizes to apical microvilli. Loss of Cad99C function results in shortened and disorganized microvilli, whereas overexpression of Cad99C leads to a dramatic increase of microvillus length. Cad99C that lacks most of the cytoplasmic domain, including potential PDZ domainbinding sites, still promotes excessive microvillus outgrowth, suggesting that the amount of the extracellular domain determines microvillus length. This study reveals Cad99C as a critical regulator of microvillus length, the first example of a transmembrane protein that is involved in this process.
Abbreviations used in this paper: CD, cadherin domain; CDH23, cadherin 23; dsRNA, double-stranded RNA; PCDH15, protocadherin 15; RNAi, RNA interference; USH1, usher syndrome type 1; VM, vitelline membrane.

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