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First published online February 8, 2005
doi: 10.1242/10.1242/jcs.01639

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Migfilin and its binding partners: from cell biology to human diseases

Department of Pathology, University of Pittsburgh, 707B Scaife Hall, 3550 Terrace Street, Pittsburgh, PA 15261, USA

View larger version (32K): [in a new window]   Fig. 1. Migfilin and its binding partners. The figure depicts migfilin domain structure, splicing variants and its binding partners. Double arrows represent direct interactions of migfilin with filamin A, B or C (mediated by the N-terminal domain of migfilin and the 21st repeat of filamin A/C (Tu et al., 2003) or the 10-13th repeats of filamin B (Takafuta et al., 2003], VASP (mediated by the central proline-rich domain of migfilin and the EVH1 domain of VASP) (Y. Zhang, Y. Tu and C.W., unpublished data), CSX/NKX2-5 (mediated by the C-terminal LIM region of migfilin and the homeodomain of CSX/NKX2-5) (Akazawa et al., 2004) and Mig-2 (mediated by the C-terminal LIM region of migfilin) (Tu et al., 2003).

View larger version (124K): [in a new window]   Fig. 2. Migfilin is clustered at cell-ECM adhesions. Human WI-38 fibroblasts were dually stained with (A) a mouse monoclonal anti-migfilin antibody (clone 43) and (B) rhodamine-phalloidin. The mouse monoclonal anti-migfilin antibody was detected with a secondary FITC-conjugated anti-mouse IgG antibody. Figure reproduced with permission from Elsevier (Tu et al., 2003).

View larger version (27K): [in a new window]   Fig. 3. Control of the subcellular localization of migfilin. The figure shows a model for the mechanism that controls migfilin localization to cell-ECM adhesions, cell-cell junctions, actin filaments and nuclei. Migfilin is recruited to cell-ECM adhesions through its interaction with Mig-2, a component of cell-ECM adhesions. In epithelial and endothelial cells, migfilin is also recruited to adherens junctions in response to cadherin-mediated cell-cell adhesion through an interaction with a yet-to-be-identified protein, which is probably a component of the cadherin–ß-catenin complex. Migfilin associates with actin filaments through its interaction with filamin, although the associations of migfilin with cell-ECM and cell-cell adhesions appear to dominate. FBLP-1, a migfilin splicing variant lacking LIM3 and therefore the ability to localize to cell-ECM or cell-cell adhesions, predominantly associates with the actin filaments. Travel of migfilin to the nucleus is regulated both by intracellular Ca2+ signaling and a nuclear export signal located within the proline-rich domain that is subjected to alternative splicing.

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