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J. Biol. Chem., Vol. 267, Issue 4, 2131-2134, Feb, 1992
AH Hirsch, SB Glantz, Y Li, Y You and CS Rubin
The A-Kinase Anchor Protein AKAP 75 (formerly designated bovine brain P75)
is a particulate brain protein that avidly binds the regulatory subunit
(RII beta) of cAMP-dependent protein kinase II beta (Bregman, D. B.,
Hirsch, A.H. and Rubin, C.S. (1991) J. Biol. Chem. 266, 7207- 7213). The
formation of stable AKAP 75.RII beta complexes provides a potential
mechanism for targeting physiological signals carried by cAMP to specific
effector sites within neurons and other brain cells. We have now cloned and
characterized the AKAP 75 gene. Its coding sequence is novel and
unexpectedly short (1284 base pairs) and contains no introns. When the AKAP
75 gene was transfected into HEK 293 cells, a new RII beta-binding protein
with an apparent Mr of 75,000 accumulated. A high proportion (approximately
65%) of the AKAP 75 gene product was excluded from the cytoplasm and was
recovered in the 40,000 x g pellet derived from disrupted transfected
cells. In contrast, cells transfected with a construct encoding 249 amino
acids from the central and C-terminal regions of AKAP 75 produced an RII
beta-binding protein (apparent Mr = 45,000) that was exclusively cytosolic.
AKAP 75 is a novel protein composed of only 428 amino acid residues (Mr =
47,878). A highly acidic C-terminal region mediates the binding of RII beta
(and cAMP-dependent protein kinase II beta), whereas a positively charged
N- terminal segment contains structural features that are essential for the
association of AKAP 75 with the cytoskeleton and/or intracellular
membranes.
Cloning and expression of an intron-less gene for AKAP 75, an anchor protein for the regulatory subunit of cAMP-dependent protein kinase II beta
Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461.
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