Crossref journal-article
Rockefeller University Press
The Journal of Cell Biology (291)
Abstract

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.

Bibliography

Robinson, D. N., & Cooley, L. (1997). Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer. The Journal of Cell Biology, 138(4), 799–810.

Authors 2
  1. Douglas N. Robinson (first)
  2. Lynn Cooley (additional)
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Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 12:47 p.m.)
Deposited 2 years, 1 month ago (July 22, 2023, 3:05 a.m.)
Indexed 1 month ago (July 30, 2025, 10:03 a.m.)
Issued 28 years ago (Aug. 25, 1997)
Published 28 years ago (Aug. 25, 1997)
Published Online 28 years ago (Aug. 25, 1997)
Published Print 28 years ago (Aug. 25, 1997)
Funders 0

None

@article{Robinson_1997, title={Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer}, volume={138}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.138.4.799}, DOI={10.1083/jcb.138.4.799}, number={4}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Robinson, Douglas N. and Cooley, Lynn}, year={1997}, month=aug, pages={799–810} }