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Vol. 16, Issue 5, 2443-2457, May 2005
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* Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520;
National Cancer Institute, National Institutes of Health, Frederick, MD 21702;
|| Department of Cell Biology, Yale University, New Haven, CT 06520; and
¶ Department of Pathology, Yale University, New Haven, CT 06520
Submitted December 23, 2004;
Revised February 14, 2005;
Accepted February 28, 2005
Monitoring Editor: Paul Matsudaira
To develop our understanding of myosin-1a function in vivo, we have created a mouse line null for the myosin-1a gene. Myosin-1a knockout mice demonstrate no overt phenotypes at the whole animal level but exhibit significant perturbations and signs of stress at the cellular level. Among these are defects in microvillar membrane morphology, distinct changes in brush-border organization, loss of numerous cytoskeletal and membrane components from the brush border, and redistribution of intermediate filament proteins into the brush border. We also observed significant ectopic recruitment of another short-tailed class I motor, myosin-1c, into the brush border of knockout enterocytes. This latter finding, a clear demonstration of functional redundancy among vertebrate myosins-I, may account for the lack of a whole animal phenotype. Nevertheless, these results indicate that myosin-1a is a critical multifunctional component of the enterocyte, required for maintaining the normal composition and highly ordered structure of the brush border.
Abbreviations used: AP, alkaline phosphatese; BB, brush border; DRM, detergent-resistant membrane; Gal4, galectin-4; MV, microvillus/i/ar; Myo, myosin; SI, sucrase isomaltase; TEM, transmission electron microscopy; SEM, scanning electron microscopy.
Present addresse: Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232;
Present addresse: Department of Biochemistry, University of Hong Kong, Hong Kong, China.
Address correspondence to: Matthew J. Tyska (matthew.tyska{at}vanderbilt.edu).
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