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Exp Cell Res. 2012 Dec 10;318(20):2543-7. doi: 10.1016/j.yexcr.2012.08.007. Epub 2012 Sep 7.

Distinct regions within fibulin-1D modulate interactions with hemicentin.

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Center for Biomedical Engineering and Technology and Department of Physiology, University of Maryland School of Medicine, University of Maryland, Baltimore 725 W. Lombard St., Baltimore, MD 21201, USA.


Fibulins are evolutionarily conserved extracellular matrix (ECM) proteins that assemble in elastic fibers and basement membranes. Caenorhabditis elegans has a single fibulin gene that produces orthologs of vertebrate fibulin-1 C and D splice forms. In a structure-function analysis of fibulin-1 domains, a series of deletion constructs show that EGF repeats 4 and 5 are required for the hemicentin-dependent assembly and function of fibulin-1D in native locations. In contrast, constructs missing the second EGF repeat of fibulin-1D (EGF2D) assemble in ectopic locations in a hemicentin dependent manner. Constructs that contain EGF2D are cleaved into two fragments, but constructs with EGF2D missing are not, suggesting that a protease binds and/or cleaves fibulin-1D at a site that is likely within EGF2D. Together, the data suggests that EGF repeats 4 and 5 promote interaction with hemicentin while a region within EGF2D suppresses ectopic interactions with hemicentin and this suppression may be protease dependent.

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