P115 IS A GENERAL VESICULAR TRANSPORT FACTOR-RELATED TO THE YEAST ENDOPLASMIC-RETICULUM TO GOLGI TRANSPORT FACTOR USO1P
P115 IS A GENERAL VESICULAR TRANSPORT FACTOR-RELATED TO THE YEAST ENDOPLASMIC-RETICULUM TO GOLGI TRANSPORT FACTOR USO1P
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DOI：
10.1073/pnas.92.2.522
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发表时间：
1995-01-17
影响因子：
11.1
通讯作者：
WATERS, MG
中科院分区：
文献类型：
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作者：
SAPPERSTEIN, SK;WALTER, DM;WATERS, MG
新近发现的囊泡转运因子p115与N-乙基马来酰亚胺敏感融合蛋白(NSF)和可溶性NSF附着蛋白一起，是高尔基体体外转运所必需的，p115是一种主要存在于高尔基体上的外周膜蛋白。生化和电子显微镜分析表明，p115是一个细长的同源二聚体，具有两个球形的头和一个延伸的尾巴，使人联想到肌球蛋白II。我们克隆并测定了牛和大鼠p115的cDNAs，预测的翻译产物有90%的同源性，每个结构域都可以分为三个结构域。预测的108 kDa牛蛋白由一个N端73 kDa的球状结构域和一个29 kDa的盘绕二聚结构域组成，一个4 kDa的连接区和一个3 kDa的高酸性结构域。p115与Uso1p有关，Uso1p是酵母内质网向Golgi囊泡运输所必需的蛋白质P115和Uso1p的头部大小相似，序列同源性接近25%，有两个高度同源性的区域(分别在34和53个残基上有62%和60%的同源性)，在螺旋线圈和酸性结构域之间有第三个同源性区域(在28个残基上有50%的同源性)，虽然p115和Uso1p C末端的酸性是保守的，但主要序列不是，我们结合p115在膜靶向和/或融合中的作用讨论了这些结果。
A recently discovered vesicular transport factor, termed p115, is required along with N-ethylmaleimide-sensitive fusion protein (NSF) and soluble NSF attachment proteins for in vitro Golgi transport, p115 is a peripheral membrane protein found predominantly on the Golgi. Biochemical and electron microscopic analyses indicate that p115 is an elongated homodimer with two globular ''heads'' and an extended ''tail'' reminiscent of myosin II, We have cloned and sequenced cDNAs for bovine and rat p115, The predicted translation products are 90% identical, and each can be divided into three domains, The predicted 108-kDa bovine protein consists of an N-terminal 73-kDa globular domain followed by a 29-kDa coiled-coil dimerization domain, a linker segment of 4 kDa, and a highly acidic domain of 3 kDa, p115 is related to Uso1p, a protein required for endoplasmic reticulum to Golgi vesicular transport in Saccharomyces cerevisiae, which has a similar ''head-coil-acid'' domain structure, The p115 and Uso1p heads are similar in size, have approximate to 25% sequence identity, and possess two highly homologous regions (62% and 60% identity over 34 and 53 residues, respectively), There is a third region of homology (50% identity over 28 residues) between the coiled-coil and acidic domains, Although the acidic nature of the p115 and Uso1p C termini is conserved, the primary sequence is not, We discuss these results in light of the proposed function of p115 in membrane targeting and/or fusion.