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Severin

A 40kDa calcium sensitive actin filament severing protein from Dictyostelium discoideum.  After a filament is severed, severin remains bound to the barbed end thereby capping the filament. Severin is homologous to fragmin a protein with similar properties from Physarum polycephalum and also to gelsolin and villin. Like these other proteins, severin is also controlled by phosphatidyl inositide containing lipids. Cells without severin were apparently normal and able to undergo the developmental cycle of the slime mould.

References:-

André, E., F. Lottspeich, et al. (1988). "Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains." J. Biol. Chem. 263, 722-728.

Eichinger, L., A. A. Noegel, et al. (1991). "Domain structure in actin-binding proteins: expression and functional characterization of truncated severin." J. Cell Biol 112, 665-676.

Eichinger, L. and M. Schleicher (1992). "Characterization of actin- and lipid-binding domains in severin, a calcium-dependent F-actin fragmenting protein." Biochemistry 31, 4779-4787.

Prendergast, G. C. and E. B. Ziff (1991). "Mbh1: a novel gelsolin/severin-related protein which binds actin in vitro and exhibits nuclear localization in vivo." EMBO Journal 10(4), 757-766.

Schnuchel, A., R. Wiltscheck, et al. (1995). "Structure of severin domain 2 in solution." J. Mol. Biol. 247, 21-27.

Yin, H. L., P. A. Janmey, et al. (1990). "Severin is a gelsolin prototype." FEBS Letters. 264, 78-80.

 
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