PUBLICATION
Identification and mapping of protein kinase A binding sites in the costameric protein myospryn
- Authors
- Reynolds, J.G., McCalmon, S.A., Tomczyk, T., and Naya, F.J.
- ID
- ZDB-PUB-070523-9
- Date
- 2007
- Source
- Biochimica et biophysica acta. Molecular cell research 1773(6): 891-902 (Journal)
- Registered Authors
- Keywords
- MEF2 target, Muscle-specific, Tripartite motif, Scaffolding protein, Costamere, Protein kinase A
- MeSH Terms
-
- A Kinase Anchor Proteins
- Amino Acid Motifs/genetics
- Animals
- COS Cells
- Carrier Proteins/genetics
- Carrier Proteins/metabolism*
- Cell Cycle Proteins/genetics
- Cell Cycle Proteins/metabolism
- Chlorocebus aethiops
- Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit
- Cyclic AMP-Dependent Protein Kinase Type II
- Cyclic AMP-Dependent Protein Kinases/metabolism*
- MEF2 Transcription Factors
- Mice
- Multiprotein Complexes/genetics
- Multiprotein Complexes/metabolism
- Muscle Proteins/genetics
- Muscle Proteins/metabolism*
- Muscle, Skeletal/cytology
- Muscle, Skeletal/metabolism*
- Myogenic Regulatory Factors/metabolism
- Peptide Mapping
- Sequence Homology, Amino Acid
- Signal Transduction/physiology*
- PubMed
- 17499862 Full text @ BBA Molecular Cell Research
Citation
Reynolds, J.G., McCalmon, S.A., Tomczyk, T., and Naya, F.J. (2007) Identification and mapping of protein kinase A binding sites in the costameric protein myospryn. Biochimica et biophysica acta. Molecular cell research. 1773(6):891-902.
Abstract
Recently we identified a novel target gene of MEF2A named myospryn that encodes a large, muscle-specific, costamere-restricted alpha-actinin binding protein. Myospryn belongs to the tripartite motif (TRIM) superfamily of proteins and was independently identified as a dysbindin-interacting protein. Dysbindin is associated with alpha-dystrobrevin, a component of the dystrophin-glycoprotein complex (DGC) in muscle. Apart from these initial findings little else is known regarding the potential function of myospryn in striated muscle. Here we reveal that myospryn is an anchoring protein for protein kinase A (PKA) (or AKAP) whose closest homolog is AKAP12, also known as gravin/AKAP250/SSeCKS. We demonstrate that myospryn co-localizes with RIIalpha, a type II regulatory subunit of PKA, at the peripheral Z-disc/costameric region in striated muscle. Myospryn interacts with RIIalpha and this scaffolding function has been evolutionarily conserved as the zebrafish ortholog also interacts with PKA. Moreover, myospryn serves as a substrate for PKA. These findings point to localized PKA signaling at the muscle costamere.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping