Journal article
D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain
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
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.
Details
- Title: Subtitle
- D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain
- Creators
- Lily Jun-shen Huang - Department of Pharmacology and Neuroscience Program, School of Medicine, University of California at San Diego, La Jolla, CA 92093-0654Kyle Durick - Department of Pharmacology and Neuroscience Program, School of Medicine, University of California at San Diego, La Jolla, CA 92093-0654Joshua A Weiner - Department of Pharmacology and Neuroscience Program, School of Medicine, University of California at San Diego, La Jolla, CA 92093-0654Jerold Chun - Department of Pharmacology and Neuroscience Program, School of Medicine, University of California at San Diego, La Jolla, CA 92093-0654Susan S Taylor - Department of Pharmacology and Neuroscience Program, School of Medicine, University of California at San Diego, La Jolla, CA 92093-0654
- Resource Type
- Journal article
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, Vol.94(21), pp.11184-11189
- DOI
- 10.1073/pnas.94.21.11184
- PMID
- 9326583
- PMCID
- PMC23409
- NLM abbreviation
- Proc Natl Acad Sci U S A
- ISSN
- 0027-8424
- eISSN
- 1091-6490
- Publisher
- National Academy of Sciences
- Language
- English
- Date published
- 10/14/1997
- Academic Unit
- Liberal Arts and Science Admin; Psychiatry; Iowa Neuroscience Institute; Biology
- Record Identifier
- 9983997436502771
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