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(Received for publication, May 16, 1997, and in revised form, July 16, 1997)
From the Activation of protein kinase A (PKA) at discrete
intracellular sites facilitates oogenesis and development in
Drosophila. Thus, PKA-anchor protein complexes may be
involved in controlling these crucial biological processes.
Evaluation of this proposition requires knowledge of PKA
binding/targeting proteins in the fly. We now report the discovery and
characterization of cDNAs encoding a novel, Drosophila
A kinase anchor protein, DAKAP550. DAKAP550 is a large (>2300 amino
acids) acidic protein that is maximally expressed in anterior tissues.
It binds regulatory subunits (RII) of both mammalian and
Drosophila PKAII isoforms. The tethering region of DAKAP550
includes two proximal, but non-contiguous RII-binding sites (B1 and
B2). The B1 domain (residues 1406-1425) binds RII ~20-fold more
avidly than B2 (amino acids 1350-1369). Affinity-purified anti-DAKAP550 IgGs were exploited to demonstrate that the anchor protein is expressed in many cells in nearly all tissues throughout the
lifespan of the fly. However, DAKAP550 is highly enriched and
asymmetrically positioned in subpopulations of neurons and in apical
portions of cells in gut and trachea. The combination of RII (PKAII)
binding activity with differential expression and polarized
localization is consistent with a role for DAKAP550 in creating target
loci for the reception of signals carried by cAMP. The DAKAP550 gene
was mapped to the 4F1.2 region of the X chromosome; flies that carry a
deletion for this portion of the X chromosome lack DAKAP550
protein.
Volume 272, Number 42,
Issue of October 17, 1997
pp. 26611-26619
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Molecular Characterization of a Novel A Kinase Anchor Protein
from Drosophila melanogaster
,
Department of Molecular Pharmacology,![]()
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