整合素细胞质结构域的膜近端区域可以介导寡聚化。

P E Zage, E E Marcantonio
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引用次数: 7

摘要

整合素-配体结合产生许多细胞内信号,包括启动局灶接触形成和调节细胞生长和分化决策的信号。β亚基细胞质结构域的寡聚化似乎是许多这些事件所必需的。为了研究这些过程,我们产生了一种新的嵌合蛋白,由鸡整合素β 1细胞质结构域连接到神经元中间丝的中央杆结构域- α -间连蛋白组成。这种嵌合蛋白在293T细胞中短暂表达时,以β细胞质结构域依赖的方式寡聚化。正如缺失分析所证明的那样,这种寡聚化需要β 1细胞质域的膜近端氨基酸LLMII。因此,该系统中的整合素β细胞质结构域包含寡聚化功能,这可能为完整整合素在体内的功能提供一些见解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The membrane proximal region of the integrin beta cytoplasmic domain can mediate oligomerization.

Integrin-ligand binding generates many intracellular signals, including signals to initiate focal contact formation and to regulate cellular decisions concerning growth and differentiation. Oligomerization of the beta subunit cytoplasmic domain appears to be required for many of these events. In order to study these processes, we have generated a novel chimeric protein, consisting of the chicken integrin beta 1 cytoplasmic domain connected to the central rod domain of a neuronal intermediate filament, alpha-internexin. This chimeric protein, when expressed transiently in 293T cells, oligomerizes in a beta cytoplasmic domain-dependent manner. This oligomerization requires the membrane proximal amino acids LLMII of the beta 1 cytoplasmic domain, as demonstrated by deletion analysis. Therefore, the integrin beta cytoplasmic domain in this system contains an oligomerization function, which may provide some insight as to the function of intact integrins in vivo.

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