| pubmed-article:21220294 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21220294 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:21220294 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:21220294 | lifeskim:mentions | umls-concept:C2931355 | lld:lifeskim |
| pubmed-article:21220294 | lifeskim:mentions | umls-concept:C1420348 | lld:lifeskim |
| pubmed-article:21220294 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:21220294 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:21220294 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:21220294 | pubmed:dateCreated | 2011-2-9 | lld:pubmed |
| pubmed-article:21220294 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21220294 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21220294 | pubmed:abstractText | The large GTPase atlastin belongs to the dynamin superfamily that has been widely implicated in facilitating membrane tubulation, fission, and in select cases, fusion. Mutations spread across atlastin isoform 1 (atlastin-1) have been identified in patients suffering from hereditary spastic paraplegia (HSP), a neurodegenerative disorder affecting motor neuron function in the lower extremities. On a molecular level, atlastin-1 associates with high membrane curvature and fusion events at the endoplasmic reticulum and cis-Golgi. Here we report crystal structures of atlastin-1 comprising the G and middle domains in two different conformations. Although the orientation of the middle domain relative to the G domain is different in the two structures, both reveal dimeric assemblies with a common, GDP-bound G domain dimer. In contrast, dimer formation in solution is observed only in the presence of GTP and transition state analogs, similar to other G proteins that are activated by nucleotide-dependent dimerization. Analyses of solution scattering data suggest that upon nucleotide binding, the protein adopts a somewhat extended, dimeric conformation that is reminiscent of one of the two crystal structures. These structural studies suggest a model for nucleotide-dependent regulation of atlastin with implications for membrane fusion. This mechanism is affected in several mutants associated with HSP, providing insights into disease pathogenesis. | lld:pubmed |
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| pubmed-article:21220294 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21220294 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21220294 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21220294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:21220294 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21220294 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:21220294 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:21220294 | pubmed:author | pubmed-author:SondermannHol... | lld:pubmed |
| pubmed-article:21220294 | pubmed:author | pubmed-author:ByrnesLaura... | lld:pubmed |
| pubmed-article:21220294 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21220294 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:21220294 | pubmed:volume | 108 | lld:pubmed |
| pubmed-article:21220294 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21220294 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21220294 | pubmed:pagination | 2216-21 | lld:pubmed |
| pubmed-article:21220294 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:21220294 | pubmed:meshHeading | pubmed-meshheading:21220294... | lld:pubmed |
| pubmed-article:21220294 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21220294 | pubmed:articleTitle | Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A. | lld:pubmed |
| pubmed-article:21220294 | pubmed:affiliation | Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA. | lld:pubmed |
| pubmed-article:21220294 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21220294 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:21220294 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21220294 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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