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J. Biol. Chem., Vol. 276, Issue 40, 37250-37257, October 5, 2001
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From the Departments of In vitro experiments showing the
activation of the myosin phosphatase via heterophilic leucine zipper
interactions between its targeting subunit (MYPT1) and
cGMP-dependent protein kinase I suggested a pathway for
smooth muscle relaxation (Surks, H. K., Mochizuki, N., Kasai, Y.,
Georgescu, S. P., Tang, K. M., Ito, M., Lincoln, T. M.,
and Mendelsohn, M. E. (1999) Science 286, 1583-1587).
The relationship between MYPT1 isoform expression and smooth muscle
responses to cGMP signaling in vivo has not been explored.
MYPT1 isoforms that contain or lack a C-terminal leucine zipper are
generated in birds and mammals by cassette-type alternative splicing of
a 31-nucleotide exon. The avian and mammalian C-terminal isoforms are
highly conserved and expressed in a tissue-specific fashion. In the
mature chicken the tonic contracting aorta and phasic contracting
gizzard exclusively express the leucine zipper positive and negative
MYPT1 isoforms, respectively. Expression of the MYPT1 isoforms is also
developmentally regulated in the gizzard, which switches from leucine
zipper positive to negative isoforms around the time of hatching. This
switch coincides with the development in the gizzard of a
cGMP-resistant phenotype, i.e. inability to dephosphorylate
myosin and relax in response to 8-bromo-cGMP after calcium activation.
Furthermore, association of cGMP-dependent protein kinase I
with MYPT1 is detected by immunoprecipitation only in the tissue that
expresses the leucine zipper positive isoform of MYPT1. These results
suggest that the regulated splicing of MYPT1 is an important
determinant of smooth muscle phenotypic diversity and the variability
in the response of smooth muscles to the calcium desensitizing effect
of cGMP signaling.
Role of Myosin Phosphatase Isoforms in cGMP-mediated Smooth
Muscle Relaxation*
§,,¶
, and¶**
Medicine (Cardiology) and
¶ Physiology and Biophysics, Case Western Reserve University
School of Medicine, Cleveland, Ohio 44106-4958
*
This work was presented in part at the Biophysical
Society Meeting, 2000 (72) and 2001 (73).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.
Supported by National Institutes of Health Grant RO1 HL64137.
**
Supported by National Institute of Health Grant RO1 HL66171-01 and
KO8 HL03275-05. To whom correspondence should be addressed: 422 BRB,
2109 Adelbert Rd., Cleveland, OH 44106-4958. Tel.: 216-368-0488; Fax:
216-368-0507; E-mail: saf9@po.cwru.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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