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PMID: 10090729 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Uncoupling integrin adhesion and signaling: the betaPS cytoplasmic domain is sufficient to regulate gene expression in the Drosophila embryo.

Genes & development ·Vol. 13 ·No. 6 ·1999-03-15 ·Pages 729-39

Martin-Bermudo MD, Brown NH

Abstract

Integrin cell surface receptors are ideally suited to coordinate cellular differentiation and tissue assembly during embryogenesis, as they can mediate both signaling and adhesion. We show that integrins regulate gene expression in the intact developing embryo by identifying two genes that require integrin function for their normal expression in Drosophila midgut endodermal cells. We determined the relative roles of integrin adhesion versus signaling in the regulation of these integrin target genes. We find that integrin-mediated adhesion is not required between the endodermal cells and the surrounding visceral mesoderm for integrin target gene expression. In addition, a chimeric protein that lacks integrin-adhesive function, but maintains the ability to signal, can substitute for the endogenous integrin and regulate integrin target genes. This chimera consists of an oligomeric extracellular domain fused to the integrin betaPS subunit cytoplasmic domain; a control monomeric extracellular domain fusion does not alter integrin target gene expression. Therefore, oligomerization of the 47-amino-acid betaPS intracellular domain is sufficient to initiate a signaling pathway that regulates gene expression in the developing embryo.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cell Adhesion/physiology Cytoplasm/metabolism DNA Primers Drosophila/embryology Drosophila Proteins Endoderm/cytology Gene Expression Regulation, Developmental/physiology Integrin alpha Chains Integrins/genetics,metabolism,physiology Mesoderm/cytology Molecular Sequence Data Recombinant Fusion Proteins/genetics,metabolism Signal Transduction
Chemicals
DNA Primers Drosophila Proteins Integrin alpha Chains Integrins Recombinant Fusion Proteins if protein, Drosophila
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Martin-Bermudo M D
Wellcome Trust/Cancer Research Campaign Institute of Cancer and Developmental Biology, and Department of Anatomy, University of Cambridge, Cambridge CB2 1QR, UK.
Brown N H
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Article Info
Journal
Genes & development
Abbr.
Genes Dev
ISSN
0890-9369
Published
1999-03-15
Pages
729-39
Language
English
Region
United States
NLM ID
8711660
PMCID
PMC316550
Subset
IM
Grants
Wellcome Trust · United Kingdom
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