Severin is a gelsolin prototype

FEBS Letters

Janmey, P.A.²  Yin, H.L.¹  Schleicher, M.³ 

[1] Department of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, TX, USA;Hematology-Oncology Unit, Massachusetts General Hospital, and Department of Medicine, Harvard Medical School, Charlestown, MA 02129, USA;Max-Planck Institute for Biochemistry, 8033 Martinsried, FRG

关键词: Calcium ion;    Polyphosphoinositide severing protein;    Gelsolin;    Severin;    PPIs;    polyphosphoinositides;    PIP;    phosphatidyl inositol 4-monophosphate;    PIP2;    phosphatidyl inositol 4;    5-bisphosphate M1̄·cm-1;    respectively;    calculated from the number of tyrosine and tryptophan residues present in the proteins [6;    13];   

DOI  :  10.1016/0014-5793(90)80769-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A number of Ca²⁺ -activated actin filament severing proteins have been identified in eukaryotic cells of diverse lineages. Gelsolin and villin, with molecular mass of about 80–90 kDa, and severin and fragmin, with molecular mass of about 40 kDa, have been isolated from vertebrates and invertebrates, respectively. We report here a direct comparison of the functional properties of gelsolin and severin, and the finding that the actin filament severing activity of severin, like that of gelsolin, is inhibited by polyphosphoinositides. However, severin does not nucleate actin filament assembly as well as gelsolin. These characteristics are very similar to those ascribed to the NH₂,-terminal half of gelsolin, supporting the idea that they are evolutionarily related. Regulation of severin by polyphospholipids raises the possibility that it may participate in agonist-stimulated regulation of the actin cytoskeleton in Dictyostelium discoideum.

【 授权许可】

Unknown