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The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia
被引:116
作者:
Ciccarelli, FD
Proukakis, C
Patel, H
Cross, H
Azam, S
Patton, MA
Bork, P
Crosby, AH
机构:
[1] Univ London St Georges Hosp, Sch Med, Dept Med Genet, London SW17 0RE, England
[2] European Mol Biol Lab, D-69012 Heidelberg, Germany
[3] Max Delbruck Ctr Mol Med, D-13092 Berlin, Germany
[4] UCL Royal Free & Univ Coll Med Sch, Dept Clin Neurosci, London NW3 2PF, England
[5] Univ Arizona, Sch Med, Dept Ophthalmol, Tucson, AZ 85724 USA
来源:
关键词:
D O I:
10.1016/S0888-7543(03)00011-9
中图分类号:
Q81 [生物工程学(生物技术)];
Q93 [微生物学];
学科分类号:
071005 ;
0836 ;
090102 ;
100705 ;
摘要:
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.
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页码:437 / 441
页数:5
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