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J. Biol. Chem., Vol. 278, Issue 6, 3985-3991, February 7, 2003
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From the Department of Physiology, University of Maryland School of
Medicine, Baltimore, Maryland 21201
Little is known about the mechanisms that
organize the internal membrane systems in eukaryotic cells. We are
addressing this question in striated muscle, which contains two novel
systems of internal membranes, the transverse tubules and the
sarcoplasmic reticulum (SR). Small ankyrin-1 (sAnk1) is an ~17-kDa
transmembrane protein of the SR that concentrates around the Z-disks
and M-lines of each sarcomere. We used the yeast two-hybrid assay to
determine whether sAnk1 interacts with titin, a giant myofibrillar
protein that organizes the sarcomere. We found that the hydrophilic
cytoplasmic domain of sAnk1 interacted with the two most
N-terminal Ig domains of titin, ZIg1 and ZIg2, which are present at the
Z-line in situ. Both ZIg1 and ZIg2 were required for
binding activity. sAnk1 did not interact with other sequences of titin
that span the Z-disk or with Ig domains of titin near the M-line. Titin
ZIg1/2 also bound T-cap/telethonin, a 19-kDa protein of the Z-line. We
show that titin ZIg1/2 could form a three-way complex with sAnk1 and T-cap. Our results indicate that titin ZIg1/2 can bind sAnk1 in muscle
homogenates and suggest a role for these proteins in organizing the SR
around the contractile apparatus at the Z-line.
The Hydrophilic Domain of Small Ankyrin-1 Interacts with the Two
N-terminal Immunoglobulin Domains of Titin*
and
*
This work was supported in part by National Institutes of
Health Grant RO1 HL64304 (to R. J. B.).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.
Recipient of National Institutes of Health Fellowship T32
AR07293. To whom correspondence should be addressed: Dept. of
Physiology, University of Maryland School of Medicine, 685 W. Baltimore
St., Baltimore, MD 21201. Tel.: 410-706-4410; Fax: 410-706-8341;
E-mail: akons001@umaryland.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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