TY - JOUR
T1 - Identification of cGMP-Dependent protein kinase anchoring proteins (GKAPs)
AU - Vo, Ngan K.
AU - Gettemy, Jessica M.
AU - Coghlan, Vincent M.
N1 - Funding Information:
We thank Michael D. Uhler for providing PKG cDNA and our colleagues at the Neurological Sciences Institute for helpful discussions. This work was supported by NIH Grant DK 52491 to V.M.C.
PY - 1998/5/29
Y1 - 1998/5/29
N2 - To promote both efficiency and selectivity, many protein kinases and phosphatases are maintained in specific subcellular microenvironments through their association with anchoring proteins. In this study, we describe a new class of proteins, called GKAPS, that specifically bind the Type II cGMP-dependent protein kinase (PKG). GKAPs were detected in rat aorta, brain, and intestine using a protein overlay technique. The PKG binding proteins were distinct from AKAPs, proteins known to bind the cAMP-dependent protein kinase (PKA). Furthermore, a synthetic peptide that blocks association of PKA with AKAPs did not affect the PKG-GKAP interaction. Deletion mutagenesis was used to map the GKAP binding determinants within PKG to the N-terminal regulatory region. While most GKAPs were tissue-specific, a ubiquitous PKG-binding protein was detected and identified as myosin. Analysis of myosin fragments revealed that PKG binds within Subfragment 2. The results define a novel class of anchoring proteins that may target PKG for specific functional roles.
AB - To promote both efficiency and selectivity, many protein kinases and phosphatases are maintained in specific subcellular microenvironments through their association with anchoring proteins. In this study, we describe a new class of proteins, called GKAPS, that specifically bind the Type II cGMP-dependent protein kinase (PKG). GKAPs were detected in rat aorta, brain, and intestine using a protein overlay technique. The PKG binding proteins were distinct from AKAPs, proteins known to bind the cAMP-dependent protein kinase (PKA). Furthermore, a synthetic peptide that blocks association of PKA with AKAPs did not affect the PKG-GKAP interaction. Deletion mutagenesis was used to map the GKAP binding determinants within PKG to the N-terminal regulatory region. While most GKAPs were tissue-specific, a ubiquitous PKG-binding protein was detected and identified as myosin. Analysis of myosin fragments revealed that PKG binds within Subfragment 2. The results define a novel class of anchoring proteins that may target PKG for specific functional roles.
UR - http://www.scopus.com/inward/record.url?scp=0032577215&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032577215&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1998.8722
DO - 10.1006/bbrc.1998.8722
M3 - Article
C2 - 9618298
AN - SCOPUS:0032577215
SN - 0006-291X
VL - 246
SP - 831
EP - 835
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -