Identification of profilin and src homology 3 domains as binding partners for Drosophila enabled. Proc Natl Acad Sci U S A 1999 Apr 27;96(9):4977-82
Date
04/29/1999Pubmed ID
10220404Pubmed Central ID
PMC21802DOI
10.1073/pnas.96.9.4977Scopus ID
2-s2.0-0033609158 (requires institutional sign-in at Scopus site) 42 CitationsAbstract
Drosophila Enabled (Ena) was first identified as a genetic suppressor of mutations in the Abelson tyrosine kinase and subsequently was shown to be a member of the Ena/vasodilator-stimulated phosphoprotein family of proteins. All members of this family have a conserved domain organization, bind the focal adhesion protein zyxin, and localize to focal adhesions and stress fibers. Members of this family are thought to be involved in the regulation of cytoskeleton dynamics. The Ena protein sequence has multiple poly-(L-proline) residues with similarity to both profilin and src homology 3 binding sites. Here, we show that Ena can bind directly to the Drosophila homolog of profilin, chickadee. Furthermore, Ena and profilin were colocalized in spreading cultured cells. We report that the proline-rich region of Ena is responsible for this interaction as well as for mediating binding to the src homology 3 domain of the Abelson tyrosine kinase. These data support the hypothesis that Ena provides a regulated link between signal transduction and cytoskeleton assembly in the developing Drosophila embryo.
Author List
Ahern-Djamali SM, Bachmann C, Hua P, Reddy SK, Kastenmeier AS, Walter U, Hoffmann FMAuthor
Andrew Sean Kastenmeier MD Associate Professor in the Surgery department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsBinding Sites
Contractile Proteins
DNA-Binding Proteins
Drosophila
Drosophila Proteins
Gene Expression Regulation, Developmental
Insect Proteins
Microfilament Proteins
Profilins
Protein Binding
src Homology Domains