The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia
The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia
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DOI：
10.1016/s0888-7543(03)00011-9
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发表时间：
2003-04-01
期刊：
影响因子：
4.4
通讯作者：
Crosby, AH
中科院分区：
文献类型：
--
作者：
Ciccarelli, FD;Proukakis, C;Crosby, AH
多重序列比对发现，在遗传性痉挛性截瘫中突变的spartin和spastin两个分子中存在一个类似于80个氨基酸的序列结构域。该结构域对应于最近描述的功能未知的ESP结构域的稍微扩展版本，在VPS4， SKD1， RPK118和SNX15中也被发现，所有这些结构域都在内体运输中具有良好的和一致的作用。最近的功能信息表明，spastin可能参与微管相互作用。有了这些关于其可能功能的新信息，我们提出了更具描述性的名称“MIT”（包含在微管相互作用和运输分子中），并预测内体运输是其存在的所有分子的主要功能。(C) 2003 Elsevier Science（美国）版权所有。
Multiple sequence alignment has revealed the presence of a sequence domain of similar to80 amino acids in two molecules, spartin and spastin, mutated in hereditary spastic paraplegia. The domain, which corresponds to a slightly extended version of the recently described ESP domain of unknown function, was also identified in VPS4, SKD1, RPK118, and SNX15, all of which have a well established and consistent role in endosomal trafficking. Recent functional information indicates that spastin is likely to be involved in microtubule interaction. With this new information relating to its likely function, we propose the more descriptive name 'MIT' (contained within microtubule-interacting and trafficking molecules) for the domain and predict endosomal trafficking as the principal functionality of all molecules in which it is present. (C) 2003 Elsevier Science (USA). All rights reserved.