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Genes to Cells (2008) 13, 987-999. doi:10.1111/j.1365-2443.2008.01226.x
© 2008 Blackwell Publishing or its licensors

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Deficiency of Myo18B in mice results in embryonic lethality with cardiac myofibrillar aberrations

Rieko Ajima1,a, Hiroshi Akazawa2, Maho Kodama3, Fumitaka Takeshita3, Ayaka Otsuka1, Takashi Kohno1, Issei Komuro2, Takahiro Ochiya3 and Jun Yokota1,*

1 Biology Division and
3 Section for Studies on Metastasis, National Cancer Center Research Institute, Tokyo 104-0045, Japan
2 Department of Cardiovascular Science and Medicine, Chiba University Graduate School of Medicine, Chiba 260-8677, Japan

Myo18B is an unconventional myosin family protein expressed predominantly in muscle cells. Although conventional myosins are known to be localized on the A-bands and function as a molecular motor for muscle contraction, Myo18B protein was localized on the Z-lines of myofibrils in striated muscles. Like Myo18A, another 18th class of myosin, the N-terminal unique domain of the protein and not the motor domain and the coiled-coil tail is critical for its localization to F-actin in myocytes. Myo18B expression was induced by myogenic differentiation through the binding of myocyte-specific enhancer factor-2 to its promoter. Deficiency of Myo18B caused an embryonic lethality in mice accompanied by disruption of myofibrillar structures in cardiac myocytes at embryonic day 10.5. Thus, Myo18B is a unique unconventional myosin that is predominantly expressed in myocytes and whose expression is essential for the development and/or maintenance of myofibrillar structure.


Communicated by: Fuyuki Ishikawa

aCurrent address: Cell and Developmental Biology Laboratory, National Cancer Institute-Frederick, NIH, MD 21702, USA.

* Correspondence: jyokota{at}gan2.ncc.go.jp







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