Danio rerio αe-catenin is a monomeric F-actin binding protein with distinct properties from Mus musculus αe-catenin

Phillip W. Miller; Sabine Pokutta; Agnidipta Ghosh; Steven C. Almo; William I. Weis; W. James Nelson; Adam V. Kwiatkowski

doi:10.1074/jbc.M113.458406

Danio rerio αe-catenin is a monomeric F-actin binding protein with distinct properties from Mus musculus αe-catenin

Phillip W. Miller, Sabine Pokutta, Agnidipta Ghosh, Steven C. Almo, William I. Weis, W. James Nelson, Adam V. Kwiatkowski

Biochemistry

Research output: Contribution to journal › Article › peer-review

27 Scopus citations

Abstract

Background: Mammalian αE-catenin is an allosterically regulated F-actin binding protein that inhibits the Arp2/3 complex. Results: D. rerio αE-catenin is a monomer that binds β-catenin and F-actin simultaneously but does not inhibit the Arp2/3 complex. Conclusion: D. rerio αE-catenin directly links the cadherin-catenin complex to F-actin. Significance: Core functions but not regulatory properties are conserved between β-catenin orthologs.

Original language	English (US)
Pages (from-to)	22324-22332
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	288
Issue number	31
DOIs	https://doi.org/10.1074/jbc.M113.458406
State	Published - Aug 2 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "Danio rerio αe-catenin is a monomeric F-actin binding protein with distinct properties from Mus musculus αe-catenin",

abstract = "Background: Mammalian αE-catenin is an allosterically regulated F-actin binding protein that inhibits the Arp2/3 complex. Results: D. rerio αE-catenin is a monomer that binds β-catenin and F-actin simultaneously but does not inhibit the Arp2/3 complex. Conclusion: D. rerio αE-catenin directly links the cadherin-catenin complex to F-actin. Significance: Core functions but not regulatory properties are conserved between β-catenin orthologs.",

author = "Miller, {Phillip W.} and Sabine Pokutta and Agnidipta Ghosh and Almo, {Steven C.} and Weis, {William I.} and Nelson, {W. James} and Kwiatkowski, {Adam V.}",

year = "2013",

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doi = "10.1074/jbc.M113.458406",

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T1 - Danio rerio αe-catenin is a monomeric F-actin binding protein with distinct properties from Mus musculus αe-catenin

AU - Miller, Phillip W.

AU - Pokutta, Sabine

AU - Ghosh, Agnidipta

AU - Almo, Steven C.

AU - Weis, William I.

AU - Nelson, W. James

AU - Kwiatkowski, Adam V.

PY - 2013/8/2

Y1 - 2013/8/2

N2 - Background: Mammalian αE-catenin is an allosterically regulated F-actin binding protein that inhibits the Arp2/3 complex. Results: D. rerio αE-catenin is a monomer that binds β-catenin and F-actin simultaneously but does not inhibit the Arp2/3 complex. Conclusion: D. rerio αE-catenin directly links the cadherin-catenin complex to F-actin. Significance: Core functions but not regulatory properties are conserved between β-catenin orthologs.

AB - Background: Mammalian αE-catenin is an allosterically regulated F-actin binding protein that inhibits the Arp2/3 complex. Results: D. rerio αE-catenin is a monomer that binds β-catenin and F-actin simultaneously but does not inhibit the Arp2/3 complex. Conclusion: D. rerio αE-catenin directly links the cadherin-catenin complex to F-actin. Significance: Core functions but not regulatory properties are conserved between β-catenin orthologs.

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ER -

Danio rerio αe-catenin is a monomeric F-actin binding protein with distinct properties from Mus musculus αe-catenin

Abstract

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