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Originally published In Press as doi:10.1074/jbc.M000518200 on March 15, 2000
J. Biol. Chem., Vol. 275, Issue 28, 21453-21459, July 14, 2000
Analysis of CMF1 Reveals a Bone Morphogenetic
Protein-independent Component of the Cardiomyogenic Pathway*
Lil M.
Pabón-Peña,
Richard L.
Goodwin,
Linda J.
Cise, and
David
Bader
From the Program for Developmental Biology, Stahlman Cardiovascular
Research Laboratories, Division of Cardiovascular Medicine, Vanderbilt
University, Nashville, Tennessee 37232-6300
Disruption of the CMF1 function in anterior
mesoderm inhibits cardiac myogenesis in avian embryos. In the present
study, we show that CMF1 is a member of an emerging family of proteins
that includes centromeric protein-F, mitosin, and LEK1. These proteins are characterized by their large size (350 kDa), dynamic subcellular distribution, and potential functions in cell division and
differentiation. The current data suggest that CMF1 is a unique member
of this family by virtue of its restricted protein expression and
variant subcellular distribution. Immunochemical analysis demonstrates that CMF1 protein is expressed in cardiogenic cells prior to the activation of cardiac structural gene products. In addition, we show
that expression of CMF1 is not dependent on the bone morphogenetic protein (BMP) signaling pathway during development. Still, CMF1 cannot
direct cardiomyogenesis in the absence of such factors as NKX-2.5.
Taken with our previous data, this study suggests that CMF1 is a
BMP-independent component of the cardiomyogenic pathway.
*
This work was supported by National Institutes of Health
(NIH) Grants HL37617 (to D. B.) and HL09916 (to R. L. G.) and NIH Training Grant HL07723 (to L. P-P.). The Vanderbilt University Medical
College Cell Imaging Resource is supported by National Institutes of
Health Grants CA68485 and DK20593.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Stahlman
Cardiovascular Research Labs., Div. of Cardiovascular Medicine,
Vanderbilt University, Rm. 338, MRB II, 2220 Pierce Ave., Nashville, TN
37232-6300. Tel.: 615-936-1976; Fax: 615-936-3527; E-mail:
david.bader@mcmail.vanderbilt.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
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