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Cullin-3 and its adaptor protein ANKFY1 determine the surface level of integrin β1 in endothelial cells

机译：Cullin-3及其衔接蛋白ANKFY1确定内皮细胞中整合素β1的表面水平

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Angiogenesis, the formation of new blood vessels from the pre-existing vasculature, is related to numerous pathophysiological events. We previously reported that a RING ubiquitin ligase complex scaffold protein, cullin-3 (CUL3), and one of its adaptor proteins, BAZF, regulated angiogenesis in the mouse retina by suppressing Notch signaling. However, the degree of inhibition of angiogenesis was made greater by CUL3 depletion than by BAZF depletion, suggesting other roles of CUL3 in angiogenesis besides the regulation of Notch signaling. In the present study, we found that CUL3 was critical for the cell surface level of integrin β1, an essential cell adhesion molecule for angiogenesis in HUVECs. By siRNA screening of 175 BTBPs, a family of adaptor proteins for CUL3, we found that ANKFY1/Rabankyrin-5, an early endosomal BTBP, was also critical for localization of surface integrin β1 and angiogenesis. CUL3 interacted with ANKFY1 and was required for the early endosomal localization of ANKFY1. These data suggest that CUL3/ANKFY1 regulates endosomal membrane traffic of integrin β1. Our results highlight the multiple roles of CUL3 in angiogenesis, which are mediated through distinct CUL3-adaptor proteins.
机译：血管生成是由先前存在的脉管系统形成的新血管，与许多病理生理事件有关。我们以前曾报道过，RING泛素连接酶复合支架蛋白cullin-3（CUL3）及其衔接蛋白之一BAZF通过抑制Notch信号调节了小鼠视网膜的血管生成。但是，CUL3耗竭比BAZF耗竭使血管生成的抑制程度更大，这表明CUL3在Notch信号传导的调控中还具有其他作用。在本研究中，我们发现CUL3对整联蛋白β1的细胞表面水平至关重要，整联蛋白β1是HUVEC中血管生成的重要细胞粘附分子。通过对175 BTBP（CUL3的衔接蛋白家族）的siRNA筛选，我们发现ANKFY1 / Rabankyrin-5（一种早期的内体BTBP）对于表面整合素β1的定位和血管生成也至关重要。 CUL3与ANKFY1相互作用，是ANKFY1早期内体定位所必需的。这些数据表明CUL3 / ANKFY1调节整合素β1的内体膜运输。我们的研究结果突显了CUL3在血管生成中的多种作用，这些作用是通过独特的CUL3适配器蛋白介导的。

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