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J. Biol. Chem., Vol. 276, Issue 20, 17448-17454, May 18, 2001
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From the Neurological Sciences Institute, Oregon Health Sciences
University, Beaverton, Oregon 97006
The cell nucleus is structurally and functionally
organized by the nuclear matrix. We have examined whether the nuclear
cAMP-dependent protein kinase-anchoring protein
AKAP95 contains specific signals for targeting to the subnuclear
compartment and for interaction with other proteins. AKAP95 was
expressed in mammalian cells and found to localize exclusively to the
nuclear matrix. Mutational analysis was used to identify determinants
for nuclear localization and nuclear matrix targeting of AKAP95. These
sites were found to be distinct from previously identified DNA and
protein kinase A binding domains. The nuclear matrix-targeting site is
unique but conserved among members of the AKAP95 family. Direct binding of AKAP95 to isolated nuclear matrix was demonstrated in
situ and found to be dependent on the nuclear matrix-targeting
site. Moreover, Far Western blot analysis identified at least three AKAP95-binding proteins in nuclear matrix isolated from rat brain. Yeast two-hybrid cloning identified one binding partner as p68 RNA
helicase. The helicase and AKAP95 co-localized in the nuclear matrix of
mammalian cells, associated in vitro, and were precipitated as a complex from solubilized cell extracts. The results define novel
protein-protein interactions among nuclear matrix proteins and suggest
a potential role of AKAP95 as a scaffold for coordinating assembly of
hormonally responsive transcription complexes.
A-kinase-anchoring Protein AKAP95 Is Targeted to the Nuclear
Matrix and Associates with p68 RNA Helicase*
*
This work was supported by United States Public Health
Service Grant DK52491 from the National Institutes of Health (to
V. M. C.).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: Neurological Sciences
Institute, Oregon Health Sciences University, 505 N. W. 185th
Ave., Beaverton, OR 97006. Tel.: 503-418-2585; Fax: 503-418-2501; E-mail: coghlanv@ohsu.edu.
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