Recombinant Mouse Filamin-A (Flna), partial

1. FlnA and Fmn2 are likely essential to cell proliferation, differentiation and cell death in a variety of tissues and organs, further reiterating the importance of vesicle trafficking in regulation of development PMID: 29240780
2. both LRP1 and LDLR expression and agLDL uptake are regulated by P2Y2R in vascular smooth muscle cells, and agLDL uptake due to P2Y2R activation is dependent upon cytoskeletal reorganization mediated by P2Y2R binding to FLN-A PMID: 27522265
3. FlnA is a negative regulator of beta2 integrin-dependent cell adhesion and reactive oxygen species production but is required for neutrophil extracellular traps production in primary murine neutrophils PMID: 28986439
4. Here the authors report that intermediate progenitor's neuron production is enhanced by abrogating filamin function, leading to the generation of periventricular neurons independent of normal neocortical neurogenesis and neuronal migration. PMID: 27664421
5. These results show that FLNA plays crucial roles in asymmetric division during meiotic maturation by regulating ROCK-cofilin-mediated actin reorganization. PMID: 28487281
6. FlnA binding to PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes and platelets. PMID: 25838348
7. FlnA is a critical upstream element of the signaling cascade underlying the myogenic tone. PMID: 26923587
8. Bones lacking filamin A are protected from estrogen-mediated post-menopausal osteoporosis PMID: 25894069
9. findings suggest a model in which filamin A local translation following axon injury controls localized HDAC5 activity to promote axon regeneration. PMID: 26157139
10. Deletion of filamin A in endothelial cells aggravated myocardial infarction-induced left ventricle dysfunction and cardiac failure as a result of defective endothelial response PMID: 25344364
11. A new signaling set, phosphatidic acid-S6K1-FLNA-actin, sheds light into the morphogenic pathway of cytoskeletal structures that are crucial for adhesion and cell locomotion during inflammation and metastasis. PMID: 25512366
12. Filamin-A is associated with neutrophil uropod retraction. PMID: 24205360
13. a major function of FLNa in modulating ion channel abundance and membrane trafficking in neurons, thereby shaping their biophysical properties and function. PMID: 24403084
14. FLNA, a large cytoskeletal actin-binding protein, physically interacts with HIF-1alpha and promotes tumor growth and angiogenesis. PMID: 24550283
15. filamin reduces ENaC channel function through direct interaction on the cell surface PMID: 23161538
16. Heart valve interstitial cells, through a serotonin, transglutaminase, and filamin-A pathway, regulate matrix organization during fetal valve development. PMID: 22843703
17. FLNA is important for lung tumor growth and that endothelial Flna impacts local tumor growth. PMID: 22857000
18. Filamin A interacts with Big2 and overexpression of Filamin A interfers with neuronal migration. PMID: 22956851
19. Loss of filamin A expression is associated with increases in the frequency of dysmorphology and severity of ciliopathy developmental defects caused by mks3 knockdown PMID: 22121117
20. FLNa is involved in podosome stability and their organization as rosettes and three-dimensional podosomes in macrophages. PMID: 22334688
21. these data demonstrate that coordinated expression of GPIbalpha and filamin is required for efficient trafficking of either protein to the cell surface, and for production of normal-sized platelets. PMID: 22174152
22. FlnA stabilizes the platelet von Willebrand factor receptor, as surface expression of von Willebrand factor receptor components is normal on FlnA-null MKs but decreased on FlnA-null platelets. PMID: 21652675
23. Filamins A and B have a major role in the maintenance of actin-based mechanical linkages that enable endoplasmic spreading and microtubule extension as well as sustained traction forces and mature focal adhesions. PMID: 21325628
24. In mice, complete loss of Filamin A expression causes embryonic lethality with severe defects in cardiovascular formation and bone development. (Review) PMID: 21169733
25. Data show that filamin-A is robustly expressed in non-myocyte cells throughout cardiac morphogenesis including epicardial and endocardial cells, and mesenchymal cells derived by EMT from these two epithelia, as well as mesenchyme of neural crest origin. PMID: 20549728
26. findings reveal that the interaction between FlnA and Syk regulates ITAM- and ITAM-like-containing receptor signaling and platelet function PMID: 20713593
27. filamin A is required for osteoclastogenesis by regulating actin dynamics via Rho GTPases that control monocyte migration. PMID: 19929439
28. Data suggest that filamin A association with caveolin-1 promotes caveolae-mediated transport by regulating vesicle internalization, clustering, and trafficking. PMID: 19759182
29. In filamin- cells the gating kinetics of HCN1 were strongly accelerated relative to filamin+ cells. PMID: 15292205
30. T-to-A transversion that converts a tyrosine codon to a stop codon in the Flna gene (Y2388X), leading to absence of the Flna protein, male lethality, cardiac malformations and skeletal defects in female. PMID: 16825286
31. Flna-null embryos display abnormal epithelial and endothelial organization and aberrant adherens junctions in developing blood vessels, heart, brain, and other tissues PMID: 17172441
32. Review explores the pathogenesis of persistent periventricular nodular heterotopia with respect to filamin-A (FLNa) mutations with mouse models. [review] PMID: 18201775
33. This study demonstrates that P2Y(2)R/FLNa interaction selectively regulates spreading and migration of vascular SMCs. PMID: 18202316
34. Wnt5a/Ror2 activates JNK, through a process involving filamin A and PKCzeta, to regulate polarized cell migration. PMID: 18667433
35. These findings support a role for FLNa-beta1 integrin as a mechanosensitive complex that bidirectionally senses the tension of the matrix and, in turn, regulates cellular contractility and response to this matrix tension. PMID: 19458194

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STRING: 10090.ENSMUSP00000098997

UniGene: Mm.295533