期刊
CELL MOTILITY AND THE CYTOSKELETON
卷 64, 期 7, 页码 519-530出版社
WILEY-LISS
DOI: 10.1002/cm.20201
关键词
microtubule; +TIPs; microtubule-associated proteins; actin; CLASP; CLIP-170; microtubutes
类别
Cell morphogenesis requires dynamic communication between actin filaments and microtubules which is mediated, at least in part, by direct structural links between the two cytoskeletal systems. Here, we examined interaction between the CLIP-associated proteins (CLASP) CLASP1 and CLASP2, and actin filaments. We demonstrate that, in addition to a well-established association with the distal ends of microtubules, CLASP2 alpha co-localizes with stress fibers, and that both CLASP1 alpha and CLASP2 alpha co-immunoprecipitate with actin. GFP-CLASP2 alpha exhibits retrograde flow in the lamellipodia of Xenopus primary fibroblasts and in the filopodia of Xenopus spinal cord neurons. A deletion mapping analysis reveals that both the microtubule-binding domain of CLASP2 (which is homologous between all CLASPs) and the N-terminal dis1/TOG domain of CLASP2 alpha (which is homologous between alpha isoforms possess actin-binding activity. Fluorescence resonance energy transfer experiments demonstrate significant energy transfer between YFP-CLASP2 alpha and CFP-actin. Our results indicate that CLASPs function as actin/microtubule crosslinkers in interphase cells. We propose that CLASPs facilitate recognition of actin filaments by the plus ends of growing microtubules at the initial stages of actin-microtubule interaction.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据