Actin polymerization induced by calspectin, a calmodulin‐binding spectrinlike protein

FEBS Letters

Sobue, Kenji¹  Kanda, Keiko¹  Morimoto, Kouichi¹  Inui, Makoto¹  Kakiuchi, Shiro¹ 

[1] Department of Neurochemistry and Neuropharmacology, Institute of Higher Nervous Activity, Osaka University Medical School, Nakanoshima, Kita-ku, Osaka 530, Japan

关键词: Calspectin;    Actin polymerization;    Calmodulin-binding protein;    Spectrin analogue;    Cytoskeletal network;    Synapse function carbol;    EGTA;    ethylene glycol bis (β-amino-ethylether)-N;    N;    N′;    N′-tetraacetic acid;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(82)80811-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have purified from a membrane fraction of bovine brain a calmodulin-binding protein (calspectin) that shares a number of properties with erythrocyte spectrin: It has a heterodimeric structure with M _r 240 000 and 235 000 and binds to (dimeric form) or crosslinks (tetrameric form) F-actin. We show that calspectin (tetramer) is capable of inducing the polymerization of G-actin to actin filaments by increasing nucleation under conditions where actin alone polymerizes at a much slower rate. Thus, brain calspectin behaves in the same manner as erythrocyte spectrin, supporting the idea that, in conjunction with actin oligomers it comprises the cytoskeletal meshwork underlying the cytoplasmic surface of the nerve cell.

【 授权许可】

Unknown