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PMID: 21550242 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

Fusing a lasting relationship between ER tubules.

Trends in cell biology ·Vol. 21 ·No. 7 ·2011-07-00 ·Pages 416-23

Moss TJ, Daga A, McNew JA

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.

MeSH Terms
Animals Endoplasmic Reticulum/metabolism,pathology GTP-Binding Proteins/genetics,metabolism Humans Membrane Fusion Membrane Proteins/genetics,metabolism Spastic Paraplegia, Hereditary/metabolism,pathology
Chemicals
Membrane Proteins ATL1 protein, human GTP-Binding Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Moss Tyler J
Department of Biochemistry and Cell Biology, Rice University, MS601, Houston, TX 77005, USA.
Daga Andrea
McNew James A
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Article Info
Journal
Trends in cell biology
Abbr.
Trends Cell Biol
ISSN
1879-3088
Published
2011-07-00
Epub
2011-00-06
Pages
416-23
Language
English
Region
England
NLM ID
9200566
PMCID
PMC3128651
Subset
IM
Grants
NIGMS NIH HHS · R01 GM071832 · United States
NIGMS NIH HHS · R01 GM071832-05 · United States
Telethon · TCR08004 · Italy
NIGMS NIH HHS · GM071832 · United States
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