Scar/WAVE is localised at the tips of protruding lamellipodia in living cells

Scar/WAVE is localised at the tips of protruding lamellipodia in living cells
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DOI:
10.1016/s0014-5793(01)02239-6
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发表时间:
2001-03-16
期刊:
影响因子:
3.5
通讯作者:
Small, JV
Small, JV
中科院分区:
生物学3区
文献类型:
--
作者:
Hahne, P;Sechi, A;Small, JV

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细胞的运动需要细胞质突起的延伸,称为片状脂膜和丝状胞壁。延伸是由肌动蛋白通过分子复合体在这些过程的末端聚合来驱动的,这些分子复合体的特征尚待确定。我们在这里显示,在活的B16F1黑色素瘤细胞中,Wiskott-Aldrich综合征蛋白家族成员Scar1/WAVE1的绿色荧光蛋白(GFP)融合被特异性地招募到板脂末端。Scar1-GFP只招募到突起的片状脂肪细胞,丝状伪足中不存在。通过用氟化铝处理细胞,可以克服以前所描述的通过异位表达SCAR抑制板脂形成的现象,从而促进了SCAR的定位。这些发现表明,SCAR位于肌动蛋白聚合的关键位置,特别是在片状脂膜突出的过程中。(C)2001年欧洲生化学会联合会。爱思唯尔科学公司出版。版权所有。
Cell motility entails the extension of cytoplasmic processes, termed lamellipodia and filopodia. Extension is driven by actin polymerisation at the tips of these processes via molecular complexes that remain to be characterised. We show here that a green fluorescent protein (GFP) fusion of the Wiskott-Aldrich syndrome protein family member Scar1/WAVE1 is specifically recruited to the tips of lamellipodia in living B16F1 melanoma cells. Scar1-GFP was recruited only to protruding lamellipodia and was absent from filopodia. The localisation of Scar was facilitated by the finding that the formerly described inhibition of lamellipodia formation by ectopical expression of Scar, could be overcome by the treatment of cells with aluminium fluoride. These findings show that Scar is strategically located at sites of actin polymerisation specifically engaged in the protrusion of lamellipodia. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.