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© The Rockefeller University Press, 0021-9525/1997//799 $5.00
The Journal of Cell Biology, Volume 138, Number 4, , 1997 799-810

Article

Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer



Douglas N. Robinson and Lynn Cooley

Department of Genetics, Yale University School of Medicine, New Haven, Connecticut 06510

Drosophila kelch has four protein domains, two of which are found in kelch-family proteins and in numerous nonkelch proteins. In Drosophila, kelch is required to maintain ring canal organization during oogenesis. We have performed a structure–function analysis to study the function of Drosophila kelch. The amino-terminal region (NTR) regulates the timing of kelch localization to the ring canals. Without the NTR, the protein localizes precociously and destabilizes the ring canals and the germ cell membranes, leading to dominant sterility. The amino half of the protein including the BTB domain mediates dimerization. Oligomerization through the amino half of kelch might allow cross-linking of ring canal actin filaments, organizing the inner rim cytoskeleton. The kelch repeat domain is necessary and sufficient for ring canal localization and likely mediates an additional interaction, possibly with actin.

Abbreviations used in this paper: KREP, kelch repeat domain; NTR, amino-terminal region; ORF, open reading frame.

Please address all correspondence to Lynn Cooley, Department of Genetics, Yale University School of Medicine, 333 Cedar St., New Haven, CT 06510. Tel.: (203) 785-5067; Fax: (203) 785-6333; E-mail: lynn.cooley{at}yale.edu

Douglas Robinson's current address is Department of Biochemistry, Beckman Center, Stanford University, Stanford, CA 94305.


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