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首页> 外文期刊>Journal of Molecular Biology >Structural basis for autoinhibition of ESCRT-III CHMP3.
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Structural basis for autoinhibition of ESCRT-III CHMP3.

机译：ESCRT-III CHMP3自抑制的结构基础。

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摘要

Endosomal sorting complexes required for transport (ESCRT-0, ESCRT-I, ESCRT-II, and ESCRT-III) are selectively recruited to cellular membranes to exert their function in diverse processes, such as multivesicular body biogenesis, enveloped virus budding, and cytokinesis. ESCRT-III is composed of members of the charged multivesicular body protein (CHMP) family--cytosolic proteins that are targeted to membranes via yet unknown signals. Membrane targeting is thought to result in a membrane-associated protein network that presumably acts at a late budding step. Here we provide structural evidence based on small-angle X-ray scattering data that ESCRT-III CHMP3 can adopt two conformations in solution: a closed globular form that most likely represents the cytosolic conformation and an open extended conformation that might represent the activated form of CHMP3. Both the closed and open conformations of CHMP3 interact with AMSH with high affinity. Although the C-terminal region of CHMP3 is required for AMSH interaction, a peptide thereof reveals only weak binding to AMSH, suggesting that other regions of CHMP3 contribute to the high-affinity interaction. Thus, AMSH, including its MIT (microtubule interacting and transport) domain, interacts with ESCRT-III CHMP3 differently from reported Vps4 MIT domain-CHMP protein interactions.
机译：运输所需的内体分选复合物（ESCRT-0，ESCRT-I，ESCRT-II和ESCRT-III）被选择性地募集到细胞膜上，以在多种过程中发挥其功能，例如多囊体生物发生，包膜病毒出芽和胞质分裂。 ESCRT-III由带电荷的多囊泡体蛋白（CHMP）家族成员（胞质蛋白）组成，该蛋白通过未知信号靶向膜。膜靶向被认为可导致膜相关蛋白网络，该网络可能在萌芽后期起作用。在此，我们基于小角度X射线散射数据提供结构证据，表明ESCRT-III CHMP3在溶液中可采用两种构象：最可能代表胞质构象的闭合球状形式和可能代表活化形式的胞浆的开放扩展构象。 CHMP3。 CHMP3的封闭和开放构象均与AMSH发生高亲和力。尽管AMSH相互作用需要CHMP3的C端区域，但是其肽仅显示出与AMSH的弱结合，这表明CHMP3的其他区域有助于高亲和力相互作用。因此，AMSH，包括其MIT（微管相互作用和转运）域，与ESCRT-III CHMP3的相互作用不同于已报道的Vps4 MIT域-CHMP蛋白的相互作用。

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