Travis Mark A, van der Flier Arjan, Kammerer Richard A, Mould A Paul, Sonnenberg Arnoud, Humphries Martin J
School of Biological Sciences, 2.205 Stopford Building, Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, The Michael Smith Building, Oxford Road, Manchester M13 9PT, UK.
FEBS Lett. 2004 Jul 2;569(1-3):185-90. doi: 10.1016/j.febslet.2004.04.099.
Integrin-filamin binding plays an important role in adhesion-mediated control of the actin cytoskeleton. Here, using the interaction between recombinant fragments from the C-terminus of filamin A and the cytoplasmic tail of integrin beta 7 as a model, we report a negative regulatory role for filamin alternative splicing. Splice variant forms of filamin A lacking a 41-amino acid segment interacted more strongly than full-length fragments. In addition, we provide evidence that phosphorylation of the splice variant region is unlikely to represent the mechanism by which binding is reduced.
整合素-细丝蛋白结合在黏附介导的肌动蛋白细胞骨架控制中起重要作用。在此，我们以细丝蛋白A C末端的重组片段与整合素β7细胞质尾巴之间的相互作用为模型，报道了细丝蛋白可变剪接的负调控作用。缺少41个氨基酸片段的细丝蛋白A剪接变体形式比全长片段的相互作用更强。此外，我们提供的证据表明，剪接变体区域的磷酸化不太可能是结合减少的机制。
