title: Fusing a lasting relationship between ER tubules.
abstract: Atlastin is an integral membrane GTPase localized to the endoplasmic reticulum (ER). In vitro and in vivo analyses indicate that atlastin is a membrane fusogen capable of driving membrane fusion, suggesting a role in ER structure and maintenance. Interestingly, mutations in the human atlastin-1 gene, SPG3A, cause a form of autosomal dominant hereditary spastic paraplegia (HSP). The etiology of HSP is unclear, but two predominant forms of the disorder are caused by mutant proteins that affect ER structure, formation and maintenance in motor neurons. In this review, we describe the current knowledge about the molecular mechanism of atlastin function and its potential role in HSP. Greater understanding of the function of atlastin and associated proteins should provide important insight into normal ER biogenesis and maintenance, as well as the pathology of disease.
authors.affiliation: Department of Biochemistry and Cell Biology, Rice University, MS601, Houston, TX 77005, USA.
authors.forename: Tyler J
authors.initials: TJ
authors.lastname: Moss
authors.forename: Andrea
authors.initials: A
authors.lastname: Daga
authors.forename: James A
authors.initials: JA
authors.lastname: McNew
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000473:pathology; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008561:Membrane Fusion; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D015419:Spastic Paraplegia, Hereditary / Q000378:metabolism / Q000473:pathology
chemical_list: D008565:Membrane Proteins; C440006:ATL1 protein, human; D019204:GTP-Binding Proteins