Danio rerio αE-catenin Is a Monomeric F-actin Binding Protein with Distinct Properties from Mus musculus αE-catenin
- Authors
- Miller, P.W., Pokutta, S., Ghosh, A., Almo, S.C., Weis, W.I., Nelson, W.J., and Kwiatkowski, A.V.
- ID
- ZDB-PUB-130710-35
- Date
- 2013
- Source
- The Journal of biological chemistry 288(31): 22324-32 (Journal)
- Registered Authors
- Keywords
- actin, adherens junction, catenin, cell adhesion, protein evolutions
- MeSH Terms
-
- Animals
- Carrier Proteins/metabolism*
- Chromatography, Gel
- Mice
- Microfilament Proteins/metabolism*
- Native Polyacrylamide Gel Electrophoresis
- Protein Binding
- Scattering, Radiation
- Zebrafish
- alpha Catenin/metabolism*
- PubMed
- 23788645 Full text @ J. Biol. Chem.
It is unknown whether homologs of the cadherin/catenin complex have conserved structures and functions across the Metazoa. Mammalian αE-catenin is an allosterically regulated actin-binding protein that binds the cadherin/β-catenin complex as a monomer and whose dimerization potentiates F-actin association. We tested whether these functional properties are conserved in another vertebrate, the zebrafish Danio rerio. Here we show, despite 90% sequence identity, that D. rerio and M. musculus αE-catenin have striking functional differences. We demonstrate that D. rerio αE-catenin is monomeric using size exclusion chromatography, native-PAGE, and small angle X-ray scattering. D. rerio αE-catenin binds F-actin in cosedimentation assays as a monomer and as an α/β-catenin heterodimer complex. D. rerio αE-catenin also bundles F-actin as shown by negative stained transmission electron microscopy, and does not inhibit Arp2/3 complex-mediated actin nucleation in bulk polymerization assays. Thus, core properties of α-catenin function - F-actin and β-catenin binding - are conserved between mouse and zebrafish. We speculate that unique regulatory properties have evolved to match specific developmental requirements.