Ferrari Ilaria, Crespi Arianna, Scita Giorgio, Pietrini Grazia
Department of BIOMETRA; Università degli Studi di Milano; CNR-Institute of Neuroscience; Milan, Italy.
Commun Integr Biol. 2012 Nov 1;5(6):631-3. doi: 10.4161/cib.21686.
Filopodia are dynamic, actin-rich finger-like structures that protrude from the cell membrane and play important roles in cell migration and neurite initiation and outgrowth. The insulin receptor substrate protein of 53 kDa (IRSp53) and the mammalian Diaphanous members of the formin family of proteins (mDia) are two key players in the formation of filopodia and neurites. IRSp53 is an adaptor protein that acts at the membrane:actin interface, coupling membrane deformation with F-actin polymerization. mDia formin proteins, instead, can nucleate and polymerize linear actin filaments. Emerging genetic and biochemical evidence indicate that there are multiple and independent pathways leading to filopodium and neurite formation, but the precise molecular components of these pathways remain ill-defined. We recently identified the PDZ domain-containing protein LIN7 as a novel regulator of IRSp53. We further showed that the association between these two proteins is required to promote the formation of filopodia and neurites independently from mDia formin proteins, highlighting novel mechanisms of filopodia and neurite formation.
丝状伪足是动态的、富含肌动蛋白的指状结构,从细胞膜突出,在细胞迁移、神经突起始和生长中发挥重要作用。53 kDa的胰岛素受体底物蛋白(IRSp53)和formin家族蛋白中的哺乳动物Diaphanous成员(mDia)是丝状伪足和神经突形成的两个关键参与者。IRSp53是一种衔接蛋白,作用于膜与肌动蛋白的界面,将膜变形与F-肌动蛋白聚合偶联起来。相反,mDia formin蛋白可以使线性肌动蛋白丝成核并聚合。新出现的遗传学和生物化学证据表明,存在多种独立的途径导致丝状伪足和神经突形成,但这些途径的确切分子成分仍不明确。我们最近鉴定出含PDZ结构域的蛋白LIN7是IRSp53的一种新型调节因子。我们进一步表明,这两种蛋白之间的结合对于独立于mDia formin蛋白促进丝状伪足和神经突的形成是必需的,这突出了丝状伪足和神经突形成的新机制。