Publication

An approach for exploring interaction between two proteins in vivo

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Last modified
  • 02/20/2025
Type of Material
Authors
    Hiroshi Kadota, Emory UniversityGuy Benian, Emory University
Language
  • English
Date
  • 2014
Publisher
  • Frontiers
Publication Version
Copyright Statement
  • © 2014 Qadota and Benian
License
Final Published Version (URL)
Title of Journal or Parent Work
ISSN
  • 1664-042X
Volume
  • 5
Issue
  • 162
Grant/Funding Information
  • Most of the studies reported here were supported by a previous grant from the American Heart Association (11GRNT7820000).
Abstract
  • We describe a strategy for exploring the function of protein-protein interactions in striated muscle in vivo. We describe our experience using this strategy to study the interaction of UNC-112 (kindlin) with PAT-4 (integrin linked kinase). Random mutagenesis is used to generate a collection of mutants that are screened for lack of binding or gain of binding using a yeast 2-hybrid assay. The mutant proteins are then expressed in transgenic C. elegans to determine their ability to localize in the sarcomere. We emphasize two advantages of this strategy: (1) for studying the interaction of protein A with protein B, when protein A can interact with multiple proteins, and (2) it explores the function of an interaction rather than the absence of, or reduced level of, a protein as can be obtained with null mutants or knockdown by RNAi. We propose that this method can be generalized for studying the meaning of a protein-protein interaction in muscle for any system in which transgenic animals can be generated and their muscles can be imaged.
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Research Categories
  • Health Sciences, Pathology

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