Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha.
We have cloned and sequenced a 9.4-kilobase cDNA specifying a new 280-kDa protein interacting with the cytoplasmic tail of glycoprotein (Gp) Ibalpha and showing considerable homology to actin-binding protein 280 ( ABP-280) and chicken retinal filamin. We term this protein human beta-filamin. The gene for beta-filamin localizes to chromosome 3p14.3-p21.1. beta-Filamin mRNA expression was observed in many tissues and in cultured human umbilical vein endothelial cells (HUVECs); only minimal expression was detected in platelets and the megakaryocytic cell line CHRF-288. Like ABP-280, beta-filamin contains an NH2-terminal actin-binding domain, a backbone of 24 tandem repeats, and two "hinge" regions. A polyclonal antibody to the unique beta-filamin first hinge sequence identifies a strong 280-kDa band in HUVECs but only a weak band in platelets, and stains normal human endothelial cells in culture and in situ. We have confirmed the interaction of beta-filamin and GpIbalpha in platelet and HUVEC lysates. In addition, using two-hybrid analysis with deletion mutants, we have localized the binding domain for GpIbalpha in beta-filamin to residues 1862-2148, an area homologous to the GpIbalpha binding domain in ABP-280. beta-Filamin is a new member of the filamin family that may have significance for GpIbalpha function in endothelial cells and platelets.[1]References
- Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha. Takafuta, T., Wu, G., Murphy, G.F., Shapiro, S.S. J. Biol. Chem. (1998) [Pubmed]
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