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Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer
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 kel...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1997
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138045/ https://www.ncbi.nlm.nih.gov/pubmed/9265647 |
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author | Robinson, Douglas N. Cooley, Lynn |
author_facet | Robinson, Douglas N. Cooley, Lynn |
author_sort | Robinson, Douglas N. |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2138045 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1997 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21380452008-05-01 Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer Robinson, Douglas N. Cooley, Lynn J Cell Biol Article 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. The Rockefeller University Press 1997-08-25 /pmc/articles/PMC2138045/ /pubmed/9265647 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Robinson, Douglas N. Cooley, Lynn Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer |
title |
Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer |
title_full |
Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer |
title_fullStr |
Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer |
title_full_unstemmed |
Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer |
title_short |
Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer |
title_sort | drosophila kelch is an oligomeric ring canal actin organizer |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138045/ https://www.ncbi.nlm.nih.gov/pubmed/9265647 |
work_keys_str_mv | AT robinsondouglasn drosophilakelchisanoligomericringcanalactinorganizer AT cooleylynn drosophilakelchisanoligomericringcanalactinorganizer |