The membrane proximal region of the integrin beta cytoplasmic domain can mediate oligomerization.
The membrane proximal region of the integrin beta cytoplasmic domain can mediate oligomerization.
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DOI：
10.3109/15419069809010780
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发表时间：
1998-07
期刊：
影响因子：
--
通讯作者：
P. Zage;E. Marcantonio
中科院分区：
文献类型：
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作者：
P. Zage;E. Marcantonio
整合素-配体结合产生许多细胞内信号，包括启动焦点接触形成和调节有关生长和分化的细胞决策的信号。许多这些事件似乎都需要β亚基胞质结构域的寡聚化。为了研究这些过程，我们生成了一种新型嵌合蛋白，由连接到神经元中间丝 α-internexin 的中央杆结构域的鸡整合素 β1 细胞质结构域组成。该嵌合蛋白在 293T 细胞中瞬时表达时，以 β 胞质结构域依赖性方式寡聚化。这种寡聚化需要 β1 胞质结构域的膜近端氨基酸 LLMII，如删除分析所证明的。因此，该系统中的整合素β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。
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.