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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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