A Mutational Analysis of dishevelled in Drosophila Defines Novel Domains in the Dishevelled Protein as Well as Novel Suppressing Alleles of axin

A Mutational Analysis of dishevelled in Drosophila Defines Novel Domains in the Dishevelled... Andrea Penton a , Andreas Wodarz a,b , and Roel Nusse a a Howard Hughes Medical Institute, Department of Developmental Biology, Stanford University Medical School, Stanford, California 94305-5323 b Institut für Genetik Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany Corresponding author: Roel Nusse, Stanford University Medical School, Howard Hughes Medical Institute, Stanford, CA 94305-5323., rnusse@cmgm.stanford.edu (E-mail) Communicating editor: T. S CH Ü PBACH Drosophila dishevelled ( dsh ) functions in two pathways: it is necessary to transduce Wingless (Wg) signaling and it is required in planar cell polarity. To learn more about how Dsh can discriminate between these functions, we performed genetic screens to isolate additional dsh alleles and we examined the potential role of protein phosphorylation by site-directed mutagenesis. We identified two alleles with point mutations in the Dsh DEP domain that specifically disrupt planar polarity signaling. When positioned in the structure of the DEP domain, these mutations are located close to each other and to a previously identified planar polarity mutation. In addition to the requirement for the DEP domain, we found that a cluster of potential phosphorylation sites in a binding domain for the protein kinase PAR-1 is also essential for planar polarity signaling. To identify regions of dsh that are necessary for Wg signaling, we screened for mutations that modified a GMR-GAL4;UAS-dsh overexpression phenotype in the eye. We recovered many alleles of the transgene containing missense mutations, including mutations in the DIX domain and in the DEP domain, the latter group mapping separately from the planar polarity mutations. In addition, several transgenes had mutations within a domain containing a consensus sequence for an SH3-binding protein. We also recovered second-site-suppressing mutations in axin , mapping at a region that may specifically interact with overexpressed Dsh. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Genetics Genetics Society of America

A Mutational Analysis of dishevelled in Drosophila Defines Novel Domains in the Dishevelled Protein as Well as Novel Suppressing Alleles of axin

Genetics, Volume 161 (2): 747 – Jun 1, 2002

Loading next page...
 
/lp/genetics-society-of-america/a-mutational-analysis-of-dishevelled-in-drosophila-defines-novel-jWaAtYtShm
Publisher
Genetics Society of America
Copyright
Copyright © 2002 by the Genetics Society of America
ISSN
0016-6731
eISSN
1943-2631
Publisher site
See Article on Publisher Site

Abstract

Andrea Penton a , Andreas Wodarz a,b , and Roel Nusse a a Howard Hughes Medical Institute, Department of Developmental Biology, Stanford University Medical School, Stanford, California 94305-5323 b Institut für Genetik Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany Corresponding author: Roel Nusse, Stanford University Medical School, Howard Hughes Medical Institute, Stanford, CA 94305-5323., rnusse@cmgm.stanford.edu (E-mail) Communicating editor: T. S CH Ü PBACH Drosophila dishevelled ( dsh ) functions in two pathways: it is necessary to transduce Wingless (Wg) signaling and it is required in planar cell polarity. To learn more about how Dsh can discriminate between these functions, we performed genetic screens to isolate additional dsh alleles and we examined the potential role of protein phosphorylation by site-directed mutagenesis. We identified two alleles with point mutations in the Dsh DEP domain that specifically disrupt planar polarity signaling. When positioned in the structure of the DEP domain, these mutations are located close to each other and to a previously identified planar polarity mutation. In addition to the requirement for the DEP domain, we found that a cluster of potential phosphorylation sites in a binding domain for the protein kinase PAR-1 is also essential for planar polarity signaling. To identify regions of dsh that are necessary for Wg signaling, we screened for mutations that modified a GMR-GAL4;UAS-dsh overexpression phenotype in the eye. We recovered many alleles of the transgene containing missense mutations, including mutations in the DIX domain and in the DEP domain, the latter group mapping separately from the planar polarity mutations. In addition, several transgenes had mutations within a domain containing a consensus sequence for an SH3-binding protein. We also recovered second-site-suppressing mutations in axin , mapping at a region that may specifically interact with overexpressed Dsh.

Journal

GeneticsGenetics Society of America

Published: Jun 1, 2002

There are no references for this article.

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create folders to
organize your research

Export folders, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off