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.
| Original language | English |
|---|---|
| Pages (from-to) | 416-423 |
| Number of pages | 8 |
| Journal | Trends in Cell Biology |
| Volume | 21 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - Jul 2011 |
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ASJC Scopus subject areas
- Cell Biology
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Fusing a lasting relationship between ER tubules. / Moss, Tyler J.; Daga, Andrea; McNew, James A.
In: Trends in Cell Biology, Vol. 21, No. 7, 07.2011, p. 416-423.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Fusing a lasting relationship between ER tubules
AU - Moss, Tyler J.
AU - Daga, Andrea
AU - McNew, James A.
PY - 2011/7
Y1 - 2011/7
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=79959577034&partnerID=8YFLogxK
U2 - 10.1016/j.tcb.2011.03.009
DO - 10.1016/j.tcb.2011.03.009
M3 - Article
VL - 21
SP - 416
EP - 423
JO - Trends in Cell Biology
JF - Trends in Cell Biology
SN - 0962-8924
IS - 7
ER -