层粘连蛋白相互作用
中文名称
通路描述
层粘连蛋白是一类保守的多结构域三聚体基底膜蛋白家族。已描述的理论三聚体组合有很多，但只有 18 种（Domogatskaya et al. 2012, Miner 2008, Macdonald et al. 2010），层粘连蛋白 212 和/或 222 的存在（Durbeej et al. 2010）尚待进一步确认。链通过其 C 端端的螺旋结构域组装。α链还含有一个大的 C 端球状结构域，包含五个 LG 结构域（LG1-5）。N 端通常被称为短臂。这些臂具有不同数量的层粘连蛋白型表皮生长因子样（LE）重复。三聚体组装由高度特异性的螺旋结构域相互作用控制（Domogatskaya et al. 2012）。一些层粘连蛋白等位基因在结合到细胞受体或其他基质分子之前，在 N 端或 C 端被蛋白酶处理（Tzu & Marinkovitch 2008）。层粘连蛋白的细胞粘附特性主要通过α链的 G 结构域介导，与整合素、 dystroglycan、Lutheran 糖蛋白或硫酸化糖脂相互作用。α-1（Colognato-Pyke et al. 1995）和α-2链（Colognato et al. 1997）以及α-5链的球状结构域 VI（Nielsen & Yamada 2001）和 IVa（Sasaki & Timpl 2001）的 N 端球状结构域可以与几种整合素等位基因（α1β1、α2β1、α3β1 和αVβ3）结合，这使得α链在层粘连蛋白的两端都能实现细胞结合。
英文描述
Laminin interactions Laminins are a large family of conserved, multidomain trimeric basement membrane proteins. There are many theoretical trimer combinations but only 18 have been described (Domogatskaya et al. 2012, Miner 2008, Macdonald et al. 2010) and the existence of isoforms laminin-212 and/or laminin-222 (Durbeej et al. 2010) awaits further confirmation. The chains assemble through coiled-coil domains at their C-terminal end. Alpha chains additionally have a large C-terminal globular domain containing five LG subdomains (LG1-5). The N termini are often referred to as the short arms. These have varying numbers of laminin-type epidermal growth factor-like (LE) repeats. Trimer assembly is controlled by highly specific coiled-coil interactions (Domogatskaya et al. 2012). Some laminin isoforms are modified extracellularly by proteolytic processing at the N- or C-terminal ends prior to their binding to cellular receptors or other matrix molecules (Tzu & Marinkovitch 2008).
The cell adhesion properties of laminins are mediated primarily through the alpha chain G domain to integrins, dystroglycan, Lutheran glycoprotein, or sulfated glycolipids. The N-terminal globular domains of the alpha-1 (Colognato-Pyke et al. 1995) and alpha-2 chains (Colognato et al. 1997) and globular domains VI (Nielsen & Yamada 2001) and IVa (Sasaki & Timpl 2001) of the alpha-5 chain can bind to several integrin isoforms (alpha1beta1, alpha2beta1, alpha3beta1, and alphaVbeta3), which enables cell binding at both ends of laminins with these alpha chains.
The cell adhesion properties of laminins are mediated primarily through the alpha chain G domain to integrins, dystroglycan, Lutheran glycoprotein, or sulfated glycolipids. The N-terminal globular domains of the alpha-1 (Colognato-Pyke et al. 1995) and alpha-2 chains (Colognato et al. 1997) and globular domains VI (Nielsen & Yamada 2001) and IVa (Sasaki & Timpl 2001) of the alpha-5 chain can bind to several integrin isoforms (alpha1beta1, alpha2beta1, alpha3beta1, and alphaVbeta3), which enables cell binding at both ends of laminins with these alpha chains.
所含基因
30 个基因