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our 11 patients with macrothrombocytopenia related to ACTN1 mutation are characterized by an isolated autosomal dominant mild thrombocytopenia, with low bleeding tendency.
Calcium modulates calmodulin-ACTN1 interaction with and agonist-dependent internalization of the adenosine A2A receptor (show ADORA2A Proteins).
Actinin-1 binds to the C-terminus of A2B adenosine receptor (show ADORA2B Proteins) (A2BAR (show ADORA2B Proteins)) and enhances A2BAR (show ADORA2B Proteins) cell-surface expression
This suggests that a precise dosage of PC2 (show KRT6B Proteins) is necessary for an adequate mechanosensitive alpha-actinin recruitment at junctions.
The present study identified a de novo mutation in ACTA1 (show ACTA1 Proteins) (c.350A>G; p.Asn117Ser) in a Chinese patient using targetcapture sequencing of a panel containing 125 known causal genes for inherited muscle diseases.
Drp1 is in dynamic equilibrium on mitochondria in a fission-independent manner, and that fission factors such as actin filaments target productive oligomerization to fission sites.
Host cortactin, PKD1 and actin are recruited by Trypanosoma cruzi extracellular amastigotes based on experiments in fixed and live cells by time lapse confocal microscopy.
The authors show that the microtubule binding protein EB1 (end-binding protein 1), a key regulator of microtubule dynamics, can bind directly to filamentous actin (F-actin) F-actin.
Several dominantly inherited congenital macrothrombocytopenia-associated mutations that are located within the actinin-1 actin-binding domain cause increased binding of actinin-1 to actin filaments and enhance filament bundling in vitro.
Data indicate that alpha-actinin (110 kDa) autoantibody was characterized as a major target in lupus nephritis (LN) patients positive for Anti-membrane autoantibodies (MbA).
Interactions with phosphatidylinositol 4,5-bisphosphate decrease the actin polymerizing activity of Ig domain 3 of palladin (Palld (show PALLD Proteins)-Ig3).
Furthermore, this F-actin mesh network attached to the synaptic ribbons directly influences the efficiency of otoferlin-dependent exocytosis and its sensitivity to intracellular hydrostatic pressure.
These findings evidence alpha-actinin involvement in sarcomeric development, suggesting for this protein an important role in stabilizing the muscle contractile apparatus.
The C-terminal polybasic region of CYTH2 (show CYTH2 Proteins) participates in interacting directly with the EFh2 domain of ACTN1.
Actn1 differential methylation occurs in diverse mouse tissues. Authors have found no indication of an imprinted effect on gene expression of Actn1 in mice.
alpha-actinin has a role in adhesion maturation through integrin-dependent force transmission to the extracellular matrix
Alpha-actinin interaction with syndecan-4 (show SDC4 Proteins) has a role in stabilising cell-matrix adhesion.
the SRF-cofilin-actin signaling axis modulates neuronal mitochondrial function
vinculin (show VCL Proteins) engagement of adhesion receptors first activates talin or alpha-actinin, by provoking structural changes that allow their vinculin (show VCL Proteins) binding sites to swing out, which are then sufficient to bind to and activate vinculin (show VCL Proteins)
EFA6A may form a protein complex with alpha-actinin and activate ARF6 in close proximity of the actin cytoskeleton and membrane proteins in the dendritic spines
Surface biotinylation and flow cytometry assays revealed that L-type calcium channel alpha(1C) channels composed of the corresponding alpha-actinin-binding-deficient mutants result in a 35-40% reduction in surface expression compared to that of wild-type channels.
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 nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Three transcript variants encoding different isoforms have been found for this gene.
actinin, alpha 1
, alpha actinin
, F-actin cross-linking protein
, actinin 1 smooth muscle
, alpha-actinin cytoskeletal isoform
, non-muscle alpha-actinin-1
, alpha actinin 1a
, non-muscle alpha-actinin 1
, alpha-actinin 1