Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer

doi:10.1083/jcb.138.4.799

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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 arefound in kelch-family proteins and in numerous nonkelch proteins.In Drosophila, kelch is required to maintain ring canal organizationduring oogenesis. We have performed a structure–functionanalysis to study the function of Drosophila kelch. The amino-terminalregion (NTR) regulates the timing of kelch localization tothe ring canals. Without the NTR, the protein localizes precociouslyand destabilizes the ring canals and the germ cell membranes,leading to dominant sterility. The amino half of the proteinincluding the BTB domain mediates dimerization. Oligomerizationthrough the amino half of kelch might allow cross-linking ofring canal actin filaments, organizing the inner rim cytoskeleton.The kelch repeat domain is necessary and sufficient for ringcanal 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, Departmentof 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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