2k9u

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Solution NMR structure of the Filamin-migfilin complexSolution NMR structure of the Filamin-migfilin complex

Structural highlights

2k9u is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FBLI1_HUMAN] Serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. Is implicated in cell shape modulation (spreading) and motility. May participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. May also regulate the assembly of filamin-containing signaling complexes that control actin assembly. Promotes dissociation of FLNA from ITGB3 and ITGB7. Promotes activation of integrins and regulates integrin-mediated cell-cell adhesion.[1] [2] [3] [4]

Publication Abstract from PubMed

The linkage of heterodimeric (alpha/beta) integrin receptors with their extracellular matrix ligands and intracellular actin cytoskeleton is a fundamental step for controlling cell adhesion and migration. Binding of the actin-linking protein, talin, to integrin beta cytoplasmic tails (CTs) induces high affinity ligand binding (integrin activation), whereas binding of another actin-linking protein, filamin, to the integrin beta CTs negatively regulates this process by blocking the talin-integrin interaction. Here we show structurally that migfilin, a novel cytoskeletal adaptor highly enriched in the integrin adhesion sites, strongly interacts with the same region in filamin where integrin beta CTs bind. We further demonstrate that the migfilin interaction dissociates filamin from integrin and promotes the talin/integrin binding and integrin activation. Migfilin thus acts as a molecular switch to disconnect filamin from integrin for regulating integrin activation and dynamics of extracellular matrix-actin linkage.

Migfilin, a molecular switch in regulation of integrin activation.,Ithychanda SS, Das M, Ma YQ, Ding K, Wang X, Gupta S, Wu C, Plow EF, Qin J J Biol Chem. 2009 Feb 13;284(7):4713-22. doi: 10.1074/jbc.M807719200. Epub 2008, Dec 13. PMID:19074766[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Tu Y, Wu S, Shi X, Chen K, Wu C. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell. 2003 Apr 4;113(1):37-47. PMID:12679033
  2. ↑ Takafuta T, Saeki M, Fujimoto TT, Fujimura K, Shapiro SS. A new member of the LIM protein family binds to filamin B and localizes at stress fibers. J Biol Chem. 2003 Apr 4;278(14):12175-81. Epub 2002 Dec 20. PMID:12496242 doi:10.1074/jbc.M209339200
  3. ↑ Lad Y, Jiang P, Ruskamo S, Harburger DS, Ylanne J, Campbell ID, Calderwood DA. Structural basis of the migfilin-filamin interaction and competition with integrin beta tails. J Biol Chem. 2008 Dec 12;283(50):35154-63. Epub 2008 Sep 30. PMID:18829455 doi:10.1074/jbc.M802592200
  4. ↑ Ithychanda SS, Das M, Ma YQ, Ding K, Wang X, Gupta S, Wu C, Plow EF, Qin J. Migfilin, a molecular switch in regulation of integrin activation. J Biol Chem. 2009 Feb 13;284(7):4713-22. doi: 10.1074/jbc.M807719200. Epub 2008, Dec 13. PMID:19074766 doi:10.1074/jbc.M807719200
  5. ↑ Ithychanda SS, Das M, Ma YQ, Ding K, Wang X, Gupta S, Wu C, Plow EF, Qin J. Migfilin, a molecular switch in regulation of integrin activation. J Biol Chem. 2009 Feb 13;284(7):4713-22. doi: 10.1074/jbc.M807719200. Epub 2008, Dec 13. PMID:19074766 doi:10.1074/jbc.M807719200
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