ArticleMolecular and cellular biology1996
An alternative, nonkinase product of the brain-specifically expressed Ca2+/calmodulin-dependent kinase II alpha isoform gene in skeletal muscle.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 58 citations in OpenAlex.
- Exercise increases Ca2+-calmodulin-dependent protein kinase II activity in human skeletal muscle.The Journal of physiology · 2003Trial
- AeLife · 2024Article
- ERK1/2 inhibition promotes robust myotube growth via CaMKII activation resulting in myoblast-to-myotube fusion.Developmental cell · 2021Article
- Phosphorylation of α-dystrobrevin is essential for αkap accumulation and acetylcholine receptor stability.The Journal of biological chemistry · 2020Article
- Heterogeneity in human hippocampal CaMKII transcripts reveals allosteric hub-dependent regulation.Science signaling · 2020Article
- CaM Kinase: Still Inspiring at 40.Neuron · 2019Review
- Analysis of the CaMKIIα and β splice-variant distribution among brain regions reveals isoform-specific differences in holoenzyme formation.Scientific reports · 2018Article
- Genomic structural variations lead to dysregulation of important coding and non-coding RNA species in dilated cardiomyopathy.EMBO molecular medicine · 2018Article
- Vascular CaMKII: heart and brain in your arteries.American journal of physiology. Cell physiology · 2016Review
- Neurotrophic factor control of satiety and body weight.Nature reviews. Neuroscience · 2016Review
- The knockdown of αkap alters the postsynaptic apparatus of neuromuscular junctions in living mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- A role for the calmodulin kinase II-related anchoring protein (αkap) in maintaining the stability of nicotinic acetylcholine receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Alpha-kinase anchoring protein alphaKAP interacts with SERCA2A to spatially position Ca2+/calmodulin-dependent protein kinase II and modulate phospholamban phosphorylation.The Journal of biological chemistry · 2009Article
- Alternative splicing generates a CaM kinase IIbeta isoform in myocardium that targets the sarcoplasmic reticulum through a putative alphaKAP and regulates GAPDH.Molecular and cellular biochemistry · 2005Article
- Activity-dependent regulation of calcium/calmodulin-dependent protein kinase II localization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Review
- Post-natal developmental expression of alphaKAP splice variants in rabbit fast-twitch and slow-twitch skeletal muscle.Journal of muscle research and cell motility · 2004Article
- Targeting of alpha-kinase-anchoring protein (alpha KAP) to sarcoplasmic reticulum and nuclei of skeletal muscle.The Biochemical journal · 2003Article
- Alternative splicing modulates the frequency-dependent response of CaMKII to Ca(2+) oscillations.The EMBO journal · 2002Article
- Structure-function of the multifunctional Ca2+/calmodulin-dependent protein kinase II.The Biochemical journal · 2002Review
- alphaKAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle.The EMBO journal · 1998Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gene for the alpha isoform of Ca2+/calmodulin-dependent kinase II (alpha CaMKII) codes for a multifunctional protein kinase that is found exclusively in the brain. Here we show that in skeletal muscle, an alternative nonkinase product, hereafter referred to as alpha KAP (alpha CaMKII association protein), is expressed from the same gene. alpha KAP consists of a C-terminal region that is identical to the association domain of alpha CaMKII, with the exception of 11 amino acids inserted in the variable region. The N-terminal sequence of alpha KAP is highly hydrophobic and not present in any known CaMKII protein. The catalytic and regulatory domains of alpha CaMKII are missing in alpha KAP. Analysis of the exon-intron structure revealed that the alpha KAP transcript is derived from the alpha CaMKII gene by alternative promoter usage and RNA splicing. The transcriptional start site of alpha KAP mRNA is located within an intron of the alpha CaMKII gene. Therefore, the relationship between alpha KAP and alpha CaMKII is that of a gene within a gene. Immunostaining using anti-alpha KAP antibodies suggests that alpha KAP is associated with sarcomeres of skeletal muscle fibers. On the basis of its primary structure and specific location, the possible function of alpha KAP as an anchoring protein for CaMKII is discussed.
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