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Published online July 23, 2007
doi:10.1083/jcb.200609096
The Journal of Cell Biology, Vol. 178, No. 3, 387-398
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Fan et al.
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Article

 A novel Crumbs3 isoform regulates cell division and ciliogenesis via importin ß interactions

Shuling Fan1, Vanessa Fogg1, Qian Wang2, Xiao-Wei Chen3, Chia-Jen Liu1, and Ben Margolis1,2

1 Department of Internal Medicine, 2 Department of Biological Chemistry, and 3 Department of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI 48109

Correspondence to Ben Margolis: bmargoli{at}umich.edu

The Crumbs family of apical transmembrane proteins regulates apicobasal polarity via protein interactions with a conserved C-terminal sequence, ERLI. However, one of the mammalian Crumbs proteins, Crumbs3 (CRB3) has an alternate splice form with a novel C-terminal sequence ending in CLPI (CRB3-CLPI). We report that CRB3-CLPI localizes to the cilia membrane and a membrane compartment at the mitotic spindle poles. Knockdown of CRB3-CLPI leads to both a loss of cilia and a multinuclear phenotype associated with centrosomal and spindle abnormalities. Using protein purification, we find that CRB3-CLPI interacts with importin ß-1 in a Ran-regulated fashion. Importin ß-1 colocalizes with CRB3-CLPI during mitosis, and a dominant-negative form of importin ß-1 closely phenocopies CRB3-CLPI knockdown. Knockdown of importin ß-1 blocks targeting of CRB3-CLPI to the spindle poles. Our data suggest an expanded role for Crumbs proteins in polarized membrane targeting and cell division via unique interactions with importin proteins.

Abbreviations used in this paper: EST, expressed sequence tag; shRNA, short hairpin RNA; wt, wild-type.


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