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Data suggest that kindlin-2 (Kind2/Fermt2 (show FERMT2 ELISA Kits)) interacts with actin alpha 2 (Actn2) and integrin beta 1 (Itgb1 (show ITGB1 ELISA Kits)) and co-localizes to cardiac sarcomere at Z-disc; knockdown of Kind2 (show FERMT2 ELISA Kits) leads to dissociation of Actn2 and Itgb1 (show ITGB1 ELISA Kits).
Data show that alpha-Actinin 2 and CaMKIIalph (show NEXN ELISA Kits)a exist in complex with GluN2B in fo (show CAMK2 ELISA Kits)rebrain.
Data demonstrated that the Z-disk proteins, ZASP (show LDB3 ELISA Kits), titin (show TTN ELISA Kits) and vinculin (show VCL ELISA Kits) preferentially bind to alpha-actinin-2. Thus, the loss of alpha-actinin-3 (show ACTN3 ELISA Kits) changes the overall protein composition of fast fiber Z-disks and alters their elastic properties.
alpha-Actinin (show ACTN1 ELISA Kits), rapsyn (show RAPSN ELISA Kits), and surface AChR form a ternary complex.
BPAG1 (show DST ELISA Kits)-b was detectable in vitro and in vivo as a high molecular mass protein in striated (show NSDHL ELISA Kits) and heart muscle cells, co-localizing with alpha-actinin-2 and partially with the cytolinker plectin (show PLEC ELISA Kits) as well as with the intermediate filament protein desmin (show DES ELISA Kits).
demonstrate that proper membrane localization of a small-conductance Ca(2 (show CA2 ELISA Kits)+)-activated K(+) channel (show KCNC4 ELISA Kits) (SK2 (show PAPSS2 ELISA Kits) or K(Ca)2.2) is dependent on its interacting protein, alpha-actinin2, a major F-actin crosslinking protein (show MACF1 ELISA Kits).
These results provide new insights into the regulation of SK2 (show KCNN2 ELISA Kits) channel trafficking by the cytoskeletal proteins FLNA (show FLNA ELISA Kits) and alpha-actinin2, involving distinct recycling pathways
the interaction between GNE (show GNE ELISA Kits) and alpha-actinin 1 (show ACTN1 ELISA Kits) and alpha-actinin 2 occur at different sites in the alpha-actinin (show ACTN1 ELISA Kits) molecules and that for alpha-actinin 2 the interaction site is located at the C-terminus of the protein.
study strengthens the hypothesis that ACTN2 influences caries risk.
The novel heterozygous missense sequence variant ACTN2 cosegregated with a complex cardiomyopathic trait, characterized by the interplay of midapical, nonobstructive HCM, early onset of AF and AV block, as well as regional LV noncompaction.
Clinical evaluation of an Australian family revealed diverse cardiac pathologies in four affected members and genetic testing of the exome identified a pathogenic ACTN2 heterozygous variant (Ala119Thr) that co-segregated with disease.
Study reports a complete high-resolution structure of the 200 kDa alpha-actinin-2 dimer from striated (show NSDHL ELISA Kits) muscle and explore its functional implications on the biochemical and cellular level.
This study generated the genomic sequences of K88-positive and F18 (show MAMLD1 ELISA Kits)-positive porcine enteroteoxigenic E. coli (ETEC) strains and examined the phylogenetic distribution of clinical porcine ETEC strains and their plasmid-associated genetic content.
Findigs show that the F-actin-binding protein (show SHROOM3 ELISA Kits) alpha-actinin-2 targets CaMKIIalpha (show CAMK2 ELISA Kits) to F-actin in cells by binding to the CaMKII (show CAMK2G ELISA Kits) regulatory domain.
data provide functional evidence that the primary sequences of alpha-actinin-2 and alpha-actinin-3 (show ACTN3 ELISA Kits) evolved differences to optimize their functions
This is the first genome-wide linkage analysis that shows mutations in ACTN2 cause HCM
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.
actinin, alpha 2
, alpha 2 actinin
, F-actin cross-linking protein
, alpha-actinin skeletal muscle