Abstract
Kindlin-2, as an integrin-interacting protein, was known to be required for the maintenance of cardiac structure and function in zebrafish. However, the mechanism remains unclear. We found that Kindlin-2 interacts and colocalizes with α-actinin-2 at the Z-disc of mouse cardiac muscles and there Kindlin-2 also interacts with β1 integrin. Knockdown of Kindlin-2 influences the association of β1 integrin with α-actinin-2 and disrupts the structure of the Z-disc and leads to cardiac dysfunction. Our data indicated that Kindlin-2 is a novel α-actinin-2-interacting protein and plays an important role in the regulation of cardiac structure and function.
Keywords:
Cardiac structure; Kindlin-2; The Z-disc; α-Actinin-2.
Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actinin / metabolism*
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Animals
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Animals, Newborn
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Cells, Cultured
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Cytoskeletal Proteins / antagonists & inhibitors
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Cytoskeletal Proteins / genetics
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Cytoskeletal Proteins / metabolism*
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Glutathione Transferase / genetics
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Glutathione Transferase / metabolism
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Integrin beta1 / metabolism*
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Male
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Mice, Inbred ICR
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Muscle Proteins / antagonists & inhibitors
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Muscle Proteins / genetics
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Muscle Proteins / metabolism*
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Myocardial Contraction
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Myocardium / cytology
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Myocardium / metabolism*
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Myocardium / ultrastructure
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Myocytes, Cardiac / cytology
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Myocytes, Cardiac / metabolism
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Myocytes, Cardiac / ultrastructure
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Protein Transport
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RNA Interference
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Rats, Sprague-Dawley
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Sarcomeres / metabolism*
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Sarcomeres / ultrastructure
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Stroke Volume
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Ultrasonography
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Ventricular Dysfunction / diagnostic imaging
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Ventricular Dysfunction / etiology
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Ventricular Dysfunction / metabolism
Substances
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Actn2 protein, mouse
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Actn2 protein, rat
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Cytoskeletal Proteins
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Integrin beta1
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Muscle Proteins
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Recombinant Fusion Proteins
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kindlin-2 protein, mouse
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Actinin
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Glutathione Transferase