Interaction of the NG2 proteoglycan with the actin cytoskeleton

Interaction of the NG2 proteoglycan with the actin cytoskeleton
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NG2 蛋白多糖与肌动蛋白细胞骨架的相互作用

DOI:
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发表时间:
1996
影响因子:
4
通讯作者:
W. Stallcup
W. Stallcup
中科院分区:
生物学2区
文献类型:
--
作者:
Xiao;K. Dahlin‐Huppe;W. Stallcup

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NG2硫酸软骨素蛋白多糖是多种发育组织中未成熟前体细胞表达的跨膜分子。在形态扁平的紧密贴壁细胞系中,NG2以线性阵列排列在细胞表面,与细胞骨架中含有肌动蛋白和肌球蛋白的应力纤维高度共定位。相比之下,细胞骨架中的微管和中间丝表现出完全不同的组织模式,这表明NG2可能使用微丝应力纤维作为细胞骨架锚定的手段。与此一致的观察结果是,细胞松弛素D破坏了细胞骨架中应力纤维和细胞表面NG2的组织。非常相似的线性细胞表面阵列也见于其他三种被认为与肌动蛋白细胞骨架相互作用的细胞表面分子:α5β1整合素、CD44蛋白聚糖和L1神经元细胞粘附分子。由于这四种分子的细胞质结构域不同,似乎每种情况下的细胞骨架锚定可能通过不同的机制发生。这种差异的一个迹象可以在秋水仙碱处理的细胞中看到,这些细胞失去了扁平的形态,但仍然保留了肌动蛋白阳性的长卷须,作为肌动蛋白细胞骨架的残留物。NG2和α5β1与这些卷须相关,而CD44和L1则无关,这表明至少存在两种细胞表面分子亚类,它们可以与肌动蛋白细胞骨架的不同亚结构域相互作用。©1996 Wiley‐Liss, Inc。
The NG2 chondroitin sulfate proteoglycan is a membrane‐spanning molecule expressed by immature precursor cells in a variety of developing tissues. In tightly adherent cell lines with a flattened morphology, NG2 is organized on the cell surface in linear arrays that are highly co‐localized with actin and myosin‐containing stress fibers in the cytoskeleton. In contrast, microtubules and intermediate filaments in the cytoskeleton exhibit completely different patterns of organization, suggesting that NG2 may use microfilamentous stress fibers as a means of cytoskeletal anchorage. Consistent with this is the observation that cytochalasin D disrupts the organization of both stress fibers in the cytoskeleton and NG2 on the cell surface. Very similar linear cell surface arrays are also seen with three other cell surface molecules thought to interact with the actin cytoskeleton: the α5β1 integrin, the CD44 proteoglycan, and the L1 neuronal cell adhesion molecule. Since the cytoplasmic domains of these four molecules are dissimilar, it seems possible that cytoskeletal anchorage in each case may occur via different mechanisms. One indication of such differences can be seen in colchicine‐treated cells which have lost their flattened morphology but still retain long actin‐positive tendrils as remnants of the actin cytoskeleton. NG2 and α5β1 are associated with these tendrils while CD44 and L1 are not, suggesting that at least two subclasses of cell surface molecules exist which can interact with different subdomains of the actin cytoskeleton. © 1996 Wiley‐Liss, Inc.
DOI: 10.1016/0304-3991(89)90411-7
发表时间: 1989-12
期刊: The American journal of pathology
影响因子: --
作者:
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DOI: 10.1091/mbc.6.12.1819
发表时间: 1995-12-01
影响因子: 3.3
作者:
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通讯作者: STALLCUP, WB
DOI: 10.1101/sqb.1983.048.01.078
发表时间: 1983
期刊: Cold Spring Harbor symposia on quantitative biology
影响因子: --
作者:
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通讯作者: Levine,J
DOI: --
发表时间: 1991-09
期刊: Cancer research
影响因子: 11.2
作者:
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DOI: --
发表时间: 1995-05
期刊: Cancer Research
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作者:
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