(Q37761966)

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Are biological sensors modulated by their structural scaffolds? The role of the structural muscle proteins alpha-actinin-2 and alpha-actinin-3 as modulators of biological sensors

scientific article published on 31 May 2010

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scholarly article

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Europe PubMed Central

PubMed publication ID

22 August 2017

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Europe PubMed Central

Are biological sensors modulated by their structural scaffolds? The role of the structural muscle proteins alpha-actinin-2 and alpha-actinin-3 as modulators of biological sensors (English)

1 reference

Europe PubMed Central

PubMed publication ID

22 August 2017

2

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Kathryn N North

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Europe PubMed Central

PubMed publication ID

22 August 2017

author name string

Monkol Lek

1

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Europe PubMed Central

PubMed publication ID

22 August 2017

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publication date

31 May 2010

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Europe PubMed Central

PubMed publication ID

22 August 2017

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Europe PubMed Central

PubMed publication ID

22 August 2017

584

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Europe PubMed Central

PubMed publication ID

22 August 2017

14

1 reference

Europe PubMed Central

PubMed publication ID

22 August 2017

2974-2980

1 reference

Europe PubMed Central

PubMed publication ID

22 August 2017

A gene for speed? The evolution and function of alpha-actinin-3.

1 reference

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Differential expression of the actin-binding proteins, alpha-actinin-2 and -3, in different species: implications for the evolution of functional redundancy.

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Loss of ACTN3 gene function alters mouse muscle metabolism and shows evidence of positive selection in humans

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ACTN3 genotype is associated with human elite athletic performance

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An Actn3 knockout mouse provides mechanistic insights into the association between alpha-actinin-3 deficiency and human athletic performance

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Gene expression profiling of mice with genetically modified muscle glycogen content

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Transcriptome and proteome analysis of soleus muscle of hormone-sensitive lipase-null mice

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Phosphofructo-1-kinase deficiency leads to a severe cardiac and hematological disorder in addition to skeletal muscle glycogenosis

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Disruption of muscle architecture and myocardial degeneration in mice lacking desmin

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Targeted Deletion of the Muscular Dystrophy Gene myotilin Does Not Perturb Muscle Structure or Function in Mice

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Sensing stretch is fundamental

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Alpha-actinin revisited: a fresh look at an old player

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Alpha-actinin structure and regulation

1 reference

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Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function

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The evolution of skeletal muscle performance: gene duplication and divergence of human sarcomeric alpha-actinins.

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Phylogenetic analysis of gene structure and alternative splicing in alpha-actinins

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Mutations in the muscle LIM protein and α-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis

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Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy

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Titin mutations as the molecular basis for dilated cardiomyopathy

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The adenosine A2A receptor interacts with the actin-binding protein alpha-actinin

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alpha-Actinin interacts with rapsyn in agrin-stimulated AChR clustering

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alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells

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Cell membrane expression of cardiac sodium channel Na(v)1.5 is modulated by alpha-actinin-2 interaction

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Alpha-actinin associates with polycystin-2 and regulates its channel activity

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Direct binding of alpha-actinin enhances TRPP3 channel activity

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Alpha-actinin-4 is selectively required for insulin-induced GLUT4 translocation

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Phosphorylation-dependent interactions of alpha-Actinin-1/IQGAP1 with the AMPA receptor subunit GluR4

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Molecular coupling of a Ca2+-activated K+ channel to L-type Ca2+ channels via alpha-actinin2

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alpha-actinin-2 is a new component of the dystrophin-glycoprotein complex.

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Competitive binding of alpha-actinin and calmodulin to the NMDA receptor

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The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy

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Beyond the sarcomere: CSRP3 mutations cause hypertrophic cardiomyopathy

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Myocyte remodeling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein

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CRP1, a LIM domain protein implicated in muscle differentiation, interacts with alpha-actinin

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MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure

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Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation

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Mutations in alpha-actinin-2 cause hypertrophic cardiomyopathy: a genome-wide analysis

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Myogenin induces a shift of enzyme activity from glycolytic to oxidative metabolism in muscles of transgenic mice

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1 reference

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Calsarcins, a novel family of sarcomeric calcineurin-binding proteins

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Mice lacking calsarcin-1 are sensitized to calcineurin signaling and show accelerated cardiomyopathy in response to pathological biomechanical stress

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Calsarcin-2 deficiency increases exercise capacity in mice through calcineurin/NFAT activation

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A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: a common link for Z-disc myopathies

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Muscle FBPase in a complex with muscle aldolase is insensitive to AMP inhibition.

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Changes in subcellular localization of fructose 1,6-bisphosphatase during differentiation of isolated muscle satellite cells.

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10.1016/J.FEBSLET.2010.05.059

1 reference

Europe PubMed Central

PubMed publication ID

22 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

22 August 2017

ResearchGate publication ID

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