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Recycling Endosomes and Transcytosis00:58

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The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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侧载Sec18对于跨细胞环境的普遍SNARE回收是必不可少的.

Yousuf A Khan1,2,3,4, K Ian White1,2,3,4,5, Richard A Pfuetzner1,2,3,4,5

  • 1Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, USA.

bioRxiv : the preprint server for biology
|September 11, 2024
PubMed
概括

在Sec18/NSF (Sec18/N-乙烯胺胺敏感因子) 中,SNARE蛋白质复合体被分解,用于膜融合. 新结构揭示Sec18/NSF使用侧载来处理拓上受约束的SNARE,而不会展开其域.

关键词:
与各种细胞活动 (AAA+) 相关的ATPases.细胞外 (exocytosis) 是一种细胞外.敏感因子 (NSF) 对于N-乙基胺胺的敏感因子质量控制 质量控制第18节 第18节可溶性N-乙基胺敏感因子附着蛋白受体 (SNARE)冷电子显微镜的使用方法单分子光共振传输能量转移.

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科学领域:

  • 分子生物学分子生物学
  • 细胞生物学 细胞生物学
  • 蛋白质的结构和功能.

背景情况:

  • 通过形成四螺旋,SNARE蛋白调解了膜融合.
  • 根据Sec18/NSF (Sec18/N-乙烯胺胺敏感因子) 和Sec17/α-SNAP,将这些捆绑拆卸回收.
  • 之前的模型面临着SNARE域和跨膜区域的拓挑战.

研究的目的:

  • 阐明Sec18/NSF在拆解SNARE复合体中的机制.
  • 通过Sec18/NSF解决SNARE基板线程的拓约束.
  • 为了可视化Sec18/NSF在拆卸周期中的结构状态.

主要方法:

  • 在体内质谱测试以确定蛋白质相互作用.
  • 电子显微镜 (Cryo-EM) 用于确定高分辨率结构.
  • 在不同功能状态下对Sec18/NSF-Sec17/α-SNAP-SNARE复合物的结构分析.

主要成果:

  • N端 SNARE 域与 Sec18/NSF 相互作用,使线程复杂化.
  • 低温EM结构显示SNARE Sso1通过Sec18/NSF的D1和D2 ATPase环进行线索.
  • Sso1 的 N-终端 Habc 域保持折叠,并与 D2 环相互作用.
  • 在水解条件下的结构显示了基质通过协调环开放释放.

结论:

  • Sec18/NSF采用侧载机制,用于引入和拆卸具有拓限制的SNARE基板.
  • 在拆卸过程中,SNARE基板不需要完全展开.
  • 这种机制允许SNARE蛋白质在随后的膜融合事件中得到有效的回收.