作为肌动蛋白网络重塑因子的 GMF。
GMF as an Actin Network Remodeling Factor.
机构信息
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South Street, Waltham, MA 02454 USA.
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South Street, Waltham, MA 02454 USA.
出版信息
Trends Cell Biol. 2018 Sep;28(9):749-760. doi: 10.1016/j.tcb.2018.04.008. Epub 2018 May 18.
Abstract
Glia maturation factor (GMF) has recently been established as a regulator of the actin cytoskeleton with a unique role in remodeling actin network architecture. Conserved from yeast to mammals, GMF is one of five members of the ADF-H family of actin regulatory proteins, which includes ADF/cofilin, Abp1/Drebrin, Twinfilin, and Coactosin. GMF does not bind actin, but instead binds the Arp2/3 complex with high affinity. Through this association, GMF catalyzes the debranching of actin filament networks and inhibits actin nucleation by Arp2/3 complex. Here, we discuss GMF's emerging role in controlling actin filament spatial organization and dynamics underlying cell motility, endocytosis, and other biological processes. Further, we attempt to reconcile these functions with its earlier characterization as a cell differentiation factor.
摘要
神经胶质细胞成熟因子（GMF）最近被确定为肌动蛋白细胞骨架的调节剂，在重塑肌动蛋白网络结构方面具有独特的作用。GMF 从酵母到哺乳动物都保守存在，是肌动蛋白调节蛋白 ADF-H 家族的五个成员之一，该家族还包括 ADF/伴肌动蛋白、Abp1/微丝结合蛋白 Drebrin、双胎蛋白和 Coactosin。GMF 不结合肌动蛋白，而是以高亲和力结合 Arp2/3 复合物。通过这种结合，GMF 催化肌动蛋白丝网络的去分支，并抑制由 Arp2/3 复合物引发的肌动蛋白成核。在这里，我们讨论了 GMF 在控制细胞运动、内吞作用和其他生物过程中肌动蛋白丝空间组织和动力学方面的新作用。此外，我们试图将这些功能与其早期作为细胞分化因子的特征相协调。
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