Danio rerio αE-catenin is a monomeric F-actin binding protein with distinct properties from Mus musculus αE-catenin
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 Danio rerio and Mus musculus αE-catenin have striking functional differences. We demonstrate that D. rerio αE-catenin is monomeric by 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.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2013 |
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Erschienen: |
2013 |
Enthalten in: |
Zur Gesamtaufnahme - volume:288 |
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Enthalten in: |
The Journal of biological chemistry - 288(2013), 31 vom: 02. Aug., Seite 22324-32 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Miller, Phillip W [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 21.10.2013 Date Revised 21.10.2021 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1074/jbc.M113.458406 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM228533260 |
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520 | |a 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 Danio rerio and Mus musculus αE-catenin have striking functional differences. We demonstrate that D. rerio αE-catenin is monomeric by 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 | ||
650 | 4 | |a Comparative Study | |
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, N.I.H., Extramural | |
650 | 4 | |a Actin | |
650 | 4 | |a Adherens Junction | |
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650 | 7 | |a Microfilament Proteins |2 NLM | |
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700 | 1 | |a Ghosh, Agnidipta |e verfasserin |4 aut | |
700 | 1 | |a Almo, Steven C |e verfasserin |4 aut | |
700 | 1 | |a Weis, William I |e verfasserin |4 aut | |
700 | 1 | |a Nelson, W James |e verfasserin |4 aut | |
700 | 1 | |a Kwiatkowski, Adam V |e verfasserin |4 aut | |
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