Function
- Filamin A (FLNA) has an actin-binding domain (ABD). It crosslinks actin filaments and participates in anchoring of membrane proteins[1].
- Filamin B (FLNB) is a human cytoplasmic protein which functions similarly to FLNA and guides proper skeletal development[2].
- Filamin C (FLNC) is functionally similar and contains 3 domains: the N-terminal ABD, the C-terminal dimerization domain (DD) and a membrane glycoprotein-binding domain[3].
For more details on filamin C see Group:MUZIC:FilaminC.
Disease
Mutations in FLNA cause frontometaphyseal dysplasia, intestinal pseudo-obstruction, Melnick-Needles syndrome, otopalatodigital syndrome and periventricular heterotopia. Mutations in FLNAB cause boomerang dysplasia[4].
3D structures of filamin
Filamin 3D structures
- ↑ Clark AR, Sawyer GM, Robertson SP, Sutherland-Smith AJ. Skeletal dysplasias due to filamin A mutations result from a gain-of-function mechanism distinct from allelic neurological disorders. Hum Mol Genet. 2009 Dec 15;18(24):4791-800. Epub 2009 Sep 22. PMID:19773341 doi:10.1093/hmg/ddp442
- ↑ Sawyer GM, Clark AR, Robertson SP, Sutherland-Smith AJ. Disease-associated substitutions in the filamin B actin binding domain confer enhanced actin binding affinity in the absence of major structural disturbance: Insights from the crystal structures of filamin B actin binding domains. J Mol Biol. 2009 Jul 31;390(5):1030-47. Epub 2009 Jun 6. PMID:19505475 doi:10.1016/j.jmb.2009.06.009
- ↑ van der Flier A, Sonnenberg A. Structural and functional aspects of filamins. Biochim Biophys Acta. 2001 Apr 23;1538(2-3):99-117. PMID:11336782
- ↑ Brunetti-Pierri N, Torrado M, Fernandez Mdel C, Tello AM, Arberas CL, Cardinale A, Piccolo P, Bacino CA. Terminal osseous dysplasia with pigmentary defects (TODPD) due to a recurrent filamin A (FLNA) mutation. Mol Genet Genomic Med. 2014 Nov;2(6):467-71. doi: 10.1002/mgg3.90. Epub 2014 Aug , 8. PMID:25614868 doi:https://dx.doi.org/10.1002/mgg3.90
