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D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain
Journal article   Open access   Peer reviewed

D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain

Lily Jun-shen Huang, Kyle Durick, Joshua A Weiner, Jerold Chun and Susan S Taylor
Proceedings of the National Academy of Sciences - PNAS, Vol.94(21), pp.11184-11189
10/14/1997
DOI: 10.1073/pnas.94.21.11184
PMCID: PMC23409
PMID: 9326583
url
https://doi.org/10.1073/pnas.94.21.11184View
Published (Version of record) Open Access

Abstract

Subcellular localization directed by specific A kinase anchoring proteins (AKAPs) is a mechanism for compartmentalization of cAMP-dependent protein kinase (PKA). Using a two-hybrid screen, a novel AKAP was isolated. Because it interacts with both the type I and type II regulatory subunits, it was defined as a dual specific AKAP or D-AKAP1. Here we report the cloning and characterization of another novel cDNA isolated from that screen. This new member of the D-AKAP family, D-AKAP2, also binds both types of regulatory subunits. A message of 5 kb pairs was detected for D-AKAP2 in all embryonic stages and in all adult tissues tested. In brain, skeletal muscle, kidney, and testis, a 10-kb mRNA was identified. In testis, several small mRNAs were observed. Therefore, D-AKAP2 represents a novel family of proteins. cDNA cloning from a mouse testis library identified the full length D-AKAP2. It is composed of 372 amino acids which includes the R binding fragment, residues 333–372, at its C-terminus. Based on coprecipitation assays, the R binding domain interacts with the N-terminal dimerization domain of RIα and RIIα. A putative RGS domain was identified near the N-terminal region of D-AKAP2. The presence of this domain raises the intriguing possibility that D-AKAP2 may interact with a Gα protein thus providing a link between the signaling machinery at the plasma membrane and the downstream kinase.
Biological Sciences

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