小窝蛋白弹性蛋白样多肽融合体介导小窝微结构域的温度依赖性组装。,ACS Biomaterials Science & Engineering

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小窝蛋白弹性蛋白样多肽融合体介导小窝微结构域的温度依赖性组装。
ACS Biomaterials Science & Engineering ( IF 5.4 ) Pub Date : 2019-12-04 , DOI: 10.1021/acsbiomaterials.9b01331
David R Tyrpak ₁ , Yue Wang ₂ , Hugo Avila ₂ , Hao Guo ₂ , Runzhong Fu ₂ , Anh T Truong ₂ , Mincheol Park ₂ , Curtis T Okamoto ₂ , Sarah F Hamm-Alvarez _{2,

3} , John Andrew MacKay _{1,

2,

3}

Affiliation

小窝是由质膜中的亚微米级侵入形成的膜细胞器，并参与机械传感，细胞信号传导和胞吞作用。尽管广泛涉及生理学和病理生理学，但是需要更好的工具来阐明通过选择性激活和灭活其贩运而引起的海绵突过程的确切作用。我们的小组最近报告说，热响应弹性蛋白样多肽（ELP）可以触发以网格蛋白轻链或表皮生长因子受体功能化的基因工程蛋白微结构域的形成。该手稿是该策略调节Caveolin-1（CAV1）的第一份报告。通过将不同的ELP序列连接到CAV1，可以使用温和的加热自组装细胞内部的CAV1-ELP微结构域。自组装的温度可以通过调整ELP顺序来控制。CAV1-ELP微区的形成将霍乱毒素亚基B内在化，霍乱毒素亚基B是小窝介导的胞吞作用的常用标记。CAV1-ELPs还与Cavin-1（功能性小窝生物发生的重要组成部分）共定位。随着小凹洞菌在健康和疾病中的新兴意义以及缺乏快速，可逆地影响小洞突囊功能的特异性探针，CAV1-ELP微域成为一种新的工具，可快速探查与胞吞作用，细胞信号转导和机械传感相关的小洞菌突突相关过程功能性小窝生物发生的必要组成部分。随着小凹洞菌在健康和疾病中的新兴意义以及缺乏快速，可逆地影响小洞突囊功能的特异性探针，CAV1-ELP微域成为一种新的工具，可快速探查与胞吞作用，细胞信号转导和机械传感相关的小洞菌突突相关过程功能性小窝生物发生的必要组成部分。随着小凹洞菌在健康和疾病中的新兴意义以及缺乏快速，可逆地影响小洞突囊功能的特异性探针，CAV1-ELP微域成为一种新的工具，可快速探查与胞吞作用，细胞信号转导和机械传感相关的小洞菌突突相关过程

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Caveolin elastin-like polypeptide fusions mediate temperature-dependent assembly of caveolar microdomains.

Caveolae are membrane organelles formed by submicrometer invaginations in the plasma membrane and are involved in mechanosensing, cell signaling, and endocytosis. Although implicated broadly in physiology and pathophysiology, better tools are required to elucidate the precise role of caveolar processes through selective activation and inactivation of their trafficking. Our group recently reported that thermally responsive elastin-like polypeptides (ELPs) can trigger formation of genetically engineered protein microdomains functionalized with either clathrin-light chain or the epidermal growth factor receptor. This manuscript is the first report of this strategy to modulate Caveolin-1 (CAV1). Through attachment of different ELP sequences to CAV1, mild heating can be used to self-assemble CAV1-ELP microdomains inside of cells. The temperature of self-assembly can be controlled by tuning the ELP sequence. The formation of CAV1-ELP microdomains internalizes cholera toxin subunit B, a commonly used marker of caveolae mediated endocytosis. CAV1-ELPs also colocalize with Cavin-1, an essential component of functional caveolae biogenesis. With the emerging significance of caveolae in health and disease and the lack of specific probes to rapidly and reversibly affect caveolar function, CAV1-ELP microdomains are a new tool to rapidly probe caveolae associated processes in endocytosis, cell signaling, and mechanosensing

更新日期：2019-12-05

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