• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Nature >A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles
【24h】

A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles

机译：SNARE-适配器相互作用是网格蛋白涂层囊泡中货物识别的一种新模式。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Soluble NSF attachment protein receptors (SNAREs) are type Ⅱ transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion and must therefore be correctly partitioned between vesicle and organelle membranes. Like all other cargo, SNAREs need to be sorted into the forming vesicles by direct interaction with components of the vesicles' coats. Here we characterize the molecular details governing the sorting of a SNARE into clathrin-coated vesicles, namely the direct recognition of the three-helical bundle H_(abc) domain oi the mouse SNARE Vti1b by the human clathrin adaptor epsinR (EPNR, also known as CLINT1). Structures of each domain and of their complex show that this interaction (dissociation constant 22 μM) is mediated by surface patches composed of approximately 15 residues each, the topographies of which are dependent on each domain's overall fold. Disruption of the interface with point mutations abolishes the interaction in vitro and causes Vtilb to become relocalized to late endosomes and lysosomes. This new class of highly specific, surface-surface interaction between the clathrin coat component and the cargo is distinct from the widely observed binding of short, linear cargo motifs by the assembly polypeptide (AP) complex and GGA adaptors and is therefore not vulnerable to competition from standard motif-containing cargoes for incorporation into clathrin-coated vesicles. We propose that conceptually similar but mechanistically different interactions will direct the post-Golgi trafficking of many SNAREs.
机译：可溶性NSF附着蛋白受体（SNARE）是Ⅱ型跨膜蛋白，在为转运小泡融合提供特异性和能量方面起关键作用，因此必须在小泡和细胞器膜之间正确分配。像所有其他货物一样，SNARE需要通过与囊的外皮成分直接相互作用而被分类到形成的囊中。在这里我们表征分子细节，控制将SNARE分类为网格蛋白包被的囊泡的排序，即人网格蛋白衔接子epsinR（EPNR，也称为人NRSN）直接识别小鼠SNARE Vti1b的三螺旋束H_（abc）域CLINT1）。每个结构域及其复合物的结构表明，这种相互作用（解离常数为22μM）是由表面贴剂介导的，每个表面贴剂由大约15个残基组成，其残基取决于每个结构域的整体折叠。具有点突变的界面破坏在体外消除了相互作用，并导致Vtilb重新定位于晚期内体和溶酶体。网格蛋白外壳组分与货物之间的这种新型的高特异性，表面-表面相互作用与组装多肽（AP）复合物和GGA衔接子所广泛观察到的短而线性的货物基序的结合不同，因此不易受到竞争的影响从包含标准图案的货物中掺入网格蛋白涂层的囊泡中。我们建议，在概念上相似但在机制上不同的相互作用将指导高尔基事件后许多网罗的贩运。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号