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Actinin, alpha 2

alpha-actinin-2, ACTN2, to alpha-actinin-2
Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a muscle-specific, alpha actinin isoform that is expressed in both skeletal and cardiac muscles. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: alpha-Actinin, Actin, CAN, ACTN3, ACID
Papers on alpha-actinin-2
Analysis of the ACTN3 Heterozygous Genotype Suggests That α-Actinin-3 Controls Sarcomeric Composition and Muscle Function in a Dose-Dependent Fashion.
North et al., Sydney, Australia. In Hum Mol Genet, Jan 2016
The R577X polymorphism is associated with changes in ACTN3 expression consistent with an additive model in the human GTEx cohort, but does not influence any other muscle transcripts, including ACTN2.
RNA-seq transcriptome analysis of extensor digitorum longus and soleus muscles in large white pigs.
Yang et al., China. In Mol Genet Genomics, Dec 2015
Moreover, transcriptome comparison between EDL and Sol identified many muscle-related genes (CSRP3, ACTN2, MYL1, and MYH6) and pathways related to myofiber formation, such as focal adhesion, tight junction formation, extracellular matrix (ECM)-receptor pathway, calcium signaling, and Wnt signaling.
Right ventricular protein expression profile in end-stage heart failure.
Di Salvo et al., Nashville, United States. In Pulm Circ, Sep 2015
In all 12 hearts, the right ventricles (RVs) demonstrated differential expression of 11 proteins relative to the left ventricles (LVs), including lesser expression of CRYM, TPM1, CLU, TXNL1, and COQ9 and greater expression of TNNI3, SAAI, ERP29, ACTN2, HSPB2, and NDUFS3.
Association of the ACTN3 R577X polymorphism with glucose tolerance and gene expression of sarcomeric proteins in human skeletal muscle.
Zierath et al., Stockholm, Sweden. In Physiol Rep, Mar 2015
ACTN2 and ACTN3 mRNA expression and protein abundance was unchanged between NGT and T2D participants.
Genetic profile of hypertrophic cardiomyopathy in Tunisia: Is it different?
Olivotto et al., Monastir, Tunisia. In Glob Cardiol Sci Pract, 2014
Using the Illumina platform, a panel of 12 genes was analyzed including myosin binding protein C (MYBPC3), beta-myosin heavy chain (MYH7), regulatory and essential light chains (MYL2 and MYL3), troponin-T (TNNT2), troponin-I (TNNI3), troponin-C (TNNC1), alpha-tropomyosin (TPM1), alpha-actin (ACTC1), alpha-actinin-2 (ACTN2) as well as alfa-galactosidase (GLA), 5'-AMP-activated protein (PKRAG2), transthyretin (TTR) and lysosomal-associated membrane protein-2 (LAMP2) for exclusion of phenocopies.
The actinin family of actin cross-linking proteins - a genetic perspective.
Young et al., Cork, Ireland. In Cell Biosci, 2014
ACTN2 mutations have been linked to a range of cardiomyopathies, and ACTN4 mutations cause a kidney condition called focal segmental glomerulosclerosis.
Global Transcriptomic Profiling of Cardiac Hypertrophy and Fatty Heart Induced by Long-Term High-Energy Diet in Bama Miniature Pigs.
Li et al., Beijing, China. In Plos One, 2014
Quantitative RT-PCR assays identified several important differentially expressed heart-related genes, including STAT3, ACSL4, ATF4, FADD, PPP3CA, CD74, SLA-8, VCL, ACTN2 and FGFR1, which may be targets of further research.
ACTN3 R577X genotypes associate with Class II and deepbite malocclusions.
Sciote et al., Lille, France. In Am J Orthod Dentofacial Orthop, 2014
ACTN2 is expressed in slow type I and fast type II fibers, whereas ACTN3 is expressed only in fast fibers.
Exome sequencing identifies a mutation in the ACTN2 gene in a family with idiopathic ventricular fibrillation, left ventricular noncompaction, and sudden death.
Semsarian et al., Sydney, Australia. In Bmc Med Genet, 2013
Whole exome sequencing identified an Ala119Thr mutation in the alpha-actinin-2 (ACTN2) gene that segregated with disease.
Substrate-selective and calcium-independent activation of CaMKII by α-actinin.
Colbran et al., Nashville, United States. In J Biol Chem, 2012
Data show that alpha-Actinin 2 and CaMKIIalpha exist in complex with GluN2B in forebrain.
α-Actinin-2 deficiency results in sarcomeric defects in zebrafish that cannot be rescued by α-actinin-3 revealing functional differences between sarcomeric isoforms.
Beggs et al., Boston, United States. In Faseb J, 2012
data provide functional evidence that the primary sequences of alpha-actinin-2 and alpha-actinin-3 evolved differences to optimize their functions
Genome sequences and phylogenetic analysis of K88- and F18-positive porcine enterotoxigenic Escherichia coli.
Johnson et al., Saint Paul, United States. In J Bacteriol, 2012
This study generated the genomic sequences of K88-positive and F18-positive porcine enteroteoxigenic E. coli (ETEC) strains and examined the phylogenetic distribution of clinical porcine ETEC strains and their plasmid-associated genetic content.
Deficiency of α-actinin-3 is associated with increased susceptibility to contraction-induced damage and skeletal muscle remodeling.
North et al., Sydney, Australia. In Hum Mol Genet, 2011
Data demonstrated that the Z-disk proteins, ZASP, titin and vinculin preferentially bind to alpha-actinin-2. Thus, the loss of alpha-actinin-3 changes the overall protein composition of fast fiber Z-disks and alters their elastic properties.
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.
North et al., Sydney, Australia. In Febs Lett, 2010
Biological sensors and their ability to detect and respond to change in the cellular environment can be modulated by protein scaffolds acting within their interaction network.
Mutations in alpha-actinin-2 cause hypertrophic cardiomyopathy: a genome-wide analysis.
Semsarian et al., Australia. In J Am Coll Cardiol, 2010
This is the first genome-wide linkage analysis that shows mutations in ACTN2 cause HCM
The evolution of skeletal muscle performance: gene duplication and divergence of human sarcomeric alpha-actinins.
North et al., Sydney, Australia. In Bioessays, 2010
Despite ACTN2 and ACTN3 retaining considerable sequence similarity, it is likely that following duplication there was a divergence in function explaining why alpha-actinin-2 cannot completely compensate for the absence of alpha-actinin-3.
Telethonin and other new proteins of the Z-disc of skeletal muscle.
Valle et al., Trieste, Italy. In Iubmb Life, 2001
Apart from the well-known Z-disc proteins such as actin, cap-Z, titin, nebulin, and alpha-actinin 2, several other Z-disc proteins have been recently discovered, including telethonin and myotilin that have been linked to limb girdle muscular dystrophies.
Clustering and anchoring mechanisms of molecular constituents of postsynaptic scaffolds in dendritic spines.
Sekino et al., Maebashi, Japan. In Neurosci Res, 2001
Drebrin A and alpha-actinin-2 are two major actin-binding proteins in dendritic spines.
Pathophysiological implications of the structural organization of the excitatory synapse.
Di Luca et al., Milano, Italy. In Eur J Pharmacol, 1999
Additional clustering of NMDA receptors is provided through the binding of NRI subunits to the cytoskeletal protein alpha-actinin-2.
Competitive binding of alpha-actinin and calmodulin to the NMDA receptor.
Sheng et al., Boston, United States. In Nature, 1997
alpha-Actinin-2, a member of the spectrin/dystrophin family of actin-binding proteins, is identified here as a brain postsynaptic density protein that colocalizes in dendritic spines with NMDA receptors and the putative NMDA receptor-clustering molecule PSD-95.
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