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首页> 外文学位 >Studies on the Sorting Mechanism of the Yeast SNARE Vti1p and the Identification and Characterization of the Yeast BAR Domain Containing Protein Gvp36p.
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Studies on the Sorting Mechanism of the Yeast SNARE Vti1p and the Identification and Characterization of the Yeast BAR Domain Containing Protein Gvp36p.

机译：酵母SNARE Vti1p的分选机制研究以及含有蛋白质Gvp36p的酵母BAR结构域的鉴定与表征。

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摘要

Membrane traffic in eukaryotic cells requires the interaction between SNAREs on transport vesicles and SNAREs on target membranes. Vti1p (Vps10 interacting 1) is a yeast SNARE, which is involved in a number of transport steps as part of four different SNARE complexes. It is found in SNARE complexes which function on the Golgi, endosomes, and the vacuole. The ability of Vti1p to mediate multiple fusion steps presumably requires distinct protein sorting factors (proteins) to ensure the fidelity of its trafficking. As Vti1p regulates multiple vesicle transport steps to many different organelles, identifying its trafficking partners is a complex task that remains to be completed. To address this I have initiated a study to identify the sorting signals and pathways of Vti1p. By co-purification experiment, I found that three clathrin-associated adaptor protein complexes (APs), AP-1, AP-2 and AP-3, interact with Vti1p and facilitate its transport between the Golgi, plasma membrane and endosomal / vacuolar compartments, respectively. I have also established that the interaction between Vti1p and the APs is dependent on a D/EXXXLL-like adaptin-dependent sorting motif (D46ELFDLL52). The mutant vti1LL-AA (L51A; L52A) was not co-purified with APs. Furthermore, I found that Gga2p (a presumptive coat protein), Ent3p (a lipid-binding domain containing protein) and Gvp36p (a BAR-domain containing protein) were also involved in sorting of Vti1p.;In my related study, a yeast novel protein Gvp36p was identified as a BAR domain containing protein. BAR domains have a capacity to bind to curved membranes and therefore may participate in maintaining organelle shape and/or in stabilizing membrane deformation as a prelude to transport vesicle formation. Structure prediction and biochemical data suggest that Gvp36p contains a BAR domain. The functional analysis shows that Gvp36p is involved in multiple pathways and functions on the post-Golgi compartments associating with Ent3p, Gga2p, and APs.
机译：真核细胞中的膜运输需要运输囊泡上的SNARE与靶膜上的SNARE之间的相互作用。 Vti1p（相互作用的Vps10）是一种酵母SNARE，作为四个不同SNARE复合体的一部分参与许多运输步骤。在对高尔基体，内体和液泡起作用的SNARE复合物中发现了它。 Vti1p介导多个融合步骤的能力可能需要不同的蛋白质分选因子（蛋白质），以确保其运输的保真度。由于Vti1p调节了向许多不同细胞器的多个囊泡运输步骤，因此确定其贩运伙伴是一项复杂的任务，有待完成。为了解决这个问题，我发起了一项研究，以识别Vti1p的分类信号和途径。通过共纯化实验，我发现三种网格蛋白相关的衔接蛋白复合物（APs），AP-1，AP-2和AP-3与Vti1p相互作用并促进其在高尔基体，质膜和内体/液泡腔室之间的运输， 分别。我还确定，Vti1p与AP之间的相互作用取决于D / EXXXLL样的Adaptin依赖性排序基序（D46ELFDLL52）。突变体vti1LL-AA（L51A; L52A）未与AP共纯化。此外，我发现Gga2p（一种推定的外壳蛋白），Ent3p（一种包含脂质结合结构域的蛋白）和Gvp36p（一种包含BAR域的蛋白）也参与了Vti1p的分选。蛋白Gvp36p被鉴定为含有BAR结构域的蛋白。 BAR结构域具有结合弯曲膜的能力，因此可以作为转运小泡形成的前奏而参与维持细胞器的形状和/或稳定膜的变形。结构预测和生化数据表明，Gvp36p包含BAR结构域。功能分析表明，Gvp36p参与了与Ent3p，Gga2p和AP相关的高尔基后区室的多种途径和功能。

著录项

  • 作者

    Wen, Ya.;

  • 作者单位

    Hong Kong University of Science and Technology (Hong Kong).;

  • 授予单位 Hong Kong University of Science and Technology (Hong Kong).;
  • 学科 Biology General.;Biology Molecular.;Biology Microbiology.
  • 学位 Ph.D.
  • 年度 2009
  • 页码 122 p.
  • 总页数 122
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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