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May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis (By similarity). De plus, nous expédions EF-Hand Domain Family, Member D2 Anticorps (47) et EF-Hand Domain Family, Member D2 Kits (10) et beaucoup plus de produits pour cette protéine.
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Data demonstrate that EFhd2 shows unique structural and biological features as an EF-hand containing F-actin bundling protein. For F-actin bundling activity, structural stabilization of the EF-hand domains was found to occur in the presence of Ca2 (Montrer CA2 Protéines)+. The core region of EFhd2 maintains its structure in the absence of Ca2 (Montrer CA2 Protéines)+ ; however, changes in local conformational flexibility reduce F-actin bundling activity of EFhd2.
Phosphorylation at Ser183 of EFhd2 causes changes in the local conformational dynamics and the surface charge distribution of the actin-binding site, resulting in a re-coordination of the actin-binding sites in the dimer structure.
The results imply that EFhd2's physiological and/or pathological function could be regulated by its phosphorylation state.
EFhd2 is involved in the control of synapse development and maintenance and is linked to dementia.
Swiprosin-1 localizes to microvilli-like membrane protrusions and lamellipodia and exhibits actin-binding activity.
Swiprosin-1 is involved in regulating the accessibility of F-actin to cofilin (Montrer CFL1 Protéines) through the clustering of F-actin and the activity of Swiprosin-1 is highly dependent on its phosphorylation status at Ser183
EFhd2 may play an important role in the pathobiology of tau-mediated neurodegeneration.
the human Shu complex (hSWS1.SWSAP1 (Montrer SWSAP1 Protéines)) has an evolutionarily conserved function in homologous recombination
Its predominant presence in CD8 (Montrer CD8A Protéines) lymphocytes suggests that swiprosin-1 may be involved in functions that are important for cytotoxic lymphocytes.
These results suggest that swiprosin-1 is a PKC-beta (Montrer PRKCB Protéines) I/eta-inducible gene and it modulates mast cell activation through NF-kappaB (Montrer NFKB1 Protéines)-dependent pathway.
this study shows that EFhd2/swiprosin-1 regulates LPS (Montrer TLR4 Protéines)-induced macrophage recruitment via enhancing actin polymerization and cell migration
These results show that EFhd2 is not essential for platelet function in mice indicating that other cytoskeletal adaptors may functionally compensate its loss.
EFhd2 is a neuronal protein that interferes with kinesin-mediated transport.
a role is found for EFhd2 as a negative regulator of germinal center-dependent humoral type 2 immunity, with implications for the generation of IgE.
Characterized EFhd2's calcium binding activity. Results showed mutations of a conserved aspartate on either EF-hand motif disrupted calcium binding activity, indicating that these motifs work in pair as a functional calcium binding domain.
Swip-1 (Montrer WSB1 Protéines) provides a membrane scaffold that is required for the Syk (Montrer SYK Protéines)-, SLP-65 (Montrer BLNK Protéines)-, and PLCgamma2 (Montrer PLCG2 Protéines)-dependent BCR (Montrer BCR Protéines)-induced calcium flux.
study shows that swiprosin-1 may regulate lifespan and BCR (Montrer BCR Protéines) signaling thresholds in immature B cells
The identification of a novel calcium-binding protein (Montrer GUCA1B Protéines) associated with tau protein in terminally ill tauopathy mouse model suggests that this association may play an important physiological and/or pathological role.
May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis (By similarity). Plays a role as negative regulator of the canonical NF-kappa-B-activating branch (By similarity). Controls spontaneous apoptosis through the regulation of BCL2L1 abundance (By similarity).
EF hand domain containing 2
, EF hand domain family, member D2
, EF-hand domain-containing protein D2
, swiprosin 1
, EF-hand domain family, member D2