Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules

Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules
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DOI:
10.1091/mbc.e05-01-0042
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发表时间:
2005-06-01
影响因子:
3.3
通讯作者:
Pieters, J
Pieters, J
中科院分区:
生物学3区
文献类型:
--
作者:
Gatfield, J;Albrecht, I;Pieters, J

文献摘要

被引文献

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柯罗宁1是柯罗宁蛋白家族的一员,在白细胞中特异表达,并聚集在F-肌动蛋白细胞骨架的重排部位。在这里,我们描述了科罗宁1分子是卷曲的线圈介导的高三聚体复合体,它通过两个不同的结构域与质膜和细胞骨架结合。与细胞骨架的结合是通过N端WD重复结构域和C端卷曲线圈之间的连接区内一段带正电的残基的三聚化来介导的。相反,质膜结合既不需要卷曲的线圈,也不需要连接子结构域中的正电荷残基,这表明N末端的WD重复结构域介导了膜相互作用。柯罗宁I将白细胞细胞骨架连接到质膜的能力可能有助于将内外信号与细胞骨架的调节结合起来。
Coronin 1 is a member of the coronin protein family specifically expressed in leukocytes and accumulates at sites of rearrangements of the F-actin cytoskeleton. Here, we describe that coronin 1 molecules are coiled coil-mediated homotrimeric complexes, which associate with the plasma membrane and with the cytoskeleton via two distinct domains. Association with the cytoskeleton was mediated by trimerization of a stretch of positively charged residues within a linker region between the N-terminal, WD repeat-containing domain and the C-terminal coiled coil. In contrast, neither the coiled coil nor the positively charged residues within the linker domain were required for plasma membrane binding, suggesting that the N-terminal, WD repeat-containing domain mediates membrane interaction. The capacity of coronin I to link the leukocyte cytoskeleton to the plasma membrane may serve to integrate outside-inside signaling with modulation of the cytoskeleton.