微管相关蛋白MAP2的磷脂酰肌醇结合位点。

The phosphatidylinositol-binding site of microtubule-associated protein MAP2.

作者信息

Burns R G, Surridge C D

机构信息

Biophysics Section, Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, U.K.

出版信息

Biochem Soc Trans. 1995 Feb;23(1):41-6. doi: 10.1042/bst0230041.

DOI:10.1042/bst0230041

PMID:7758753

Abstract

Recent evidence [Surridge and Burns, Biochemistry (1994) 33, 8051-8057] on the interaction of native and recombinant tau, recombinant MAP2c, and native MAP2 with vesicles prepared from phosphatidylinositol (PtdIns) and other phospholipids demonstrate that MAP2 differs from MAP2c and from tau in having a high-affinity PtdIns-binding site. The location of this site within the MAP2-specific insert peptide, coupled with considerations of the nature of the MAP2 tubulin-binding site, suggests that PtdIns-binding induces a conformational change which alters the MAP2 tubulin-binding domain. Furthermore, the restricted cellular distribution of MAP2 implies that the MAP2:PtdIns interaction may play a central role in modulating the dendritic cytoskeleton.

摘要

最近的证据[Surridge和Burns，《生物化学》（1994年）33卷，8051 - 8057页]表明，天然和重组的tau、重组的MAP2c以及天然的MAP2与由磷脂酰肌醇（PtdIns）和其他磷脂制备的囊泡之间的相互作用显示，MAP2与MAP2c和tau不同，它具有一个高亲和力的PtdIns结合位点。该位点在MAP2特异性插入肽内的位置，结合对MAP2微管蛋白结合位点性质的考虑，表明PtdIns结合会诱导构象变化，从而改变MAP2微管蛋白结合结构域。此外，MAP2在细胞内分布受限，这意味着MAP2与PtdIns的相互作用可能在调节树突状细胞骨架中起核心作用。