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J. Biol. Chem., Vol. 276, Issue 14, 11189-11198, April 6, 2001
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From the Subcellular targeting of the components of the
cAMP-dependent pathway is thought to be essential for
intracellular signaling. Here we have identified a novel protein, named
myomegalin, that interacts with the cyclic nucleotide phosphodiesterase
PDE4D, thereby targeting it to particulate structures. Myomegalin is a
large 2,324-amino acid protein mostly composed of The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF139185.
Myomegalin Is a Novel Protein of the Golgi/Centrosome That
Interacts with a Cyclic Nucleotide Phosphodiesterase*
§,§,,,,,, and
Division of Reproductive Biology, Department
of Gynecology and Obstetrics, Stanford University School of Medicine,
Stanford, California 94305-5317 and the ¶ Department of
Immunology, Berlex Biosciences, Richmond, California 94804-0099
-helical and
coiled-coil structures, with domains shared with microtubule-associated proteins, and a leucine zipper identical to that found in the Drosophila centrosomin. Transcripts of 7.5-8 kilobases
were present in most tissues, whereas a short mRNA of 2.4 kilobases
was detected only in rat testis. A third splicing variant was expressed
predominantly in rat heart. Antibodies against the deduced sequence
recognized particulate myomegalin proteins of 62 kDa in testis and
230-250 kDa in heart and skeletal muscle. Immunocytochemistry and
transfection studies demonstrate colocalization of PDE4D and myomegalin
in the Golgi/centrosomal area of cultured cells, and in sarcomeric structures of skeletal muscle. Myomegalin expressed in COS-7 cells coimmunoprecipitated with PDE4D3 and sequestered it to particulate structures. These findings indicate that myomegalin is a novel protein
that functions as an anchor to localize components of the
cAMP-dependent pathway to the Golgi/centrosomal region
of the cell.
*
This work was supported by National Institutes of Health
Grant RO1-HD20788 and by a gift from Berlex (to G. P.).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. Tel.:
650-725-2452; Fax: 650-725-7102; E-mail:
marco.conti@stanford.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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