Disease relevance of Flna

• However, Salmonella infection of filamin-A-deficient M2 cells did not significantly differ from infection of filamin-A-containing A7 cells, ruling out the possibility that filamin-A is a major protein inhibiting Salmonella invasion and replication [1].

High impact information on Flna

• For other cytoskeletal proteins such as filamin, tropomyosin and myosin, a similar accumulation under caps was not readily apparent using whole cell mounts, although earlier experiments with frozen-sectioned cells had shown such an enrichment of myosin (as well as actin) [2].
• Here, we describe the high-resolution structure of an interface between filamin A and an integrin adhesion receptor [3].
• The molecular basis of filamin binding to integrins and competition with talin [3].
• Expression of Fln was elevated in MEKK4(-/-) forebrain, most notably near sites of failed neuronal migration [4].
• One gene product, LL5beta, binds to both phosphoinositides and a cytoskeletal protein, filamin, one form of which is concentrated at synaptic sites [5].

Biological context of Flna

• Filamin A and FILIP (Filamin A-Interacting Protein) regulate cell polarity and motility in neocortical subventricular and intermediate zones during radial migration [6].
• The similarity of the phenotype of FLNc-deficient mice to the filamin-interacting TRIO null mice was further confirmed by comparing FLNc-deficient C2C12 cells to TRIO-deficient cells [7].
• Also, in filamin- cells the gating kinetics of HCN1 were strongly accelerated relative to filamin+ cells [8].
• Filamin isogene expression during mouse myogenesis [9].
• This is the first study of filamin gene expression at the early stages of skeletal muscle development [9].

Anatomical context of Flna

• Instead, Flna-null embryos display abnormal epithelial and endothelial organization and aberrant adherens junctions in developing blood vessels, heart, brain, and other tissues [10].
• During myofibril assembly in cultured chick cardiomyocytes, N-RAP and filamin appear to co-localize with alpha-actinin in the earliest myofibril precursors found near the cell periphery, as well as in the nascent myofibrils that form as these structures fuse laterally [11].
• Furthermore, 4 weeks after disease induction, autoantibodies appeared which were reactive with laminin alpha1, beta1, beta2, and gamma1 chains, and filamin in rat mesangial cell matrix [12].
• Muscle-specific filamin transcripts had a size of 10 kb and were expressed primarily in cardiac and skeletal muscle [9].
• The results showed that muscle-specific filamin gene transcripts are detected before the formation of myotubes in vivo [9].

Associations of Flna with chemical compounds

• During the same time interval, alpha-actinin is mobilized to the cell periphery at cell "ruffles." However, 12(S)-HETE showed little or no effects on actin-binding proteins filamin and tropomyosin or on microtubules [13].

Physical interactions of Flna

• Dynamic interactions of Fc gamma receptor IIB with filamin-bound SHIP1 amplify filamentous actin-dependent negative regulation of Fc epsilon receptor I signaling [14].

Other interactions of Flna

• We addressed the mechanism by which PEBP2beta localizes to the cytoplasm and found that it is associated with filamin A, an actin-binding protein [15].
• The transcriptional organization of the region of the mouse X chromosome between the G6pd and the Fln1 genes was studied in detail, and it was compared with the syntenic region of the human chromosome [16].
• New N-RAP-binding partners alpha-actinin, filamin and Krp1 detected by yeast two-hybrid screening: implications for myofibril assembly [11].
• This article reviews the evidence (i) that the integrin beta-subunit cytoplasmic domain is important in the localization of integrins to focal adhesions, and for integrin-mediated cell adhesion/spreading; and (ii) that the integrin beta-subunit can be linked to F-actin via the actin-binding proteins talin, alpha-actinin and filamin [17].
• Based on these results, we propose a dynamic model in which the submembranous F-actin skeleton forms an inhibitory compartment where filamin-1 functions as a donor of SHIP1 for FcgammaRIIB, which concentrate this phosphatase in the vicinity of FcepsilonRI and thereby extinguish activation signals [14].

Analytical, diagnostic and therapeutic context of Flna

• We also verified by immunoprecipitation from bovine brain that the filamin A-HCN1 interaction is functional in vivo [8].
• Immunofluorescence localization of cytoskeletal proteins in distal excluding compartments indicated the presence of filament bundles containing F-actin nonmuscle filamin (ABP280) and alpha-actinin [18].
• Northern blot and in situ hybridization results showed that nonmuscle-specific filamin transcripts had a size of 9.5 kb and were expressed in all nonmuscle tissues [9].
• DNA vaccination with SmCT-SOD induced a mean of 39% protection, filamin induced a mean of 50% protection, and SmGPX induced no protection compared to controls following challenge with adult worms by surgical transfer [19].

References