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A C-terminal amphipathic helix is necessary for the in-vivo tubule-shaping function of plant reticulon
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Breeze, Emily, Dzimitrowicz, Natasha, Kriechbaumer, Verena, Brooks, Rhiannon, Botchway, Stanley W., Brady, Jacob P., Hawes, Chris, Dixon, Ann M., Schnell, Jason R., Fricker, Mark D. and Frigerio, Lorenzo (2016) A C-terminal amphipathic helix is necessary for the in-vivo tubule-shaping function of plant reticulon. Proceedings of the National Academy of Sciences of the United States of America, 113 (39). pp. 10902-10907. doi:10.1073/pnas.1605434113 ISSN 0027-8424.
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Official URL: http://dx.doi.org/10.1073/pnas.1605434113
Abstract
Reticulons (RTNs) are a class of endoplasmic reticulum (ER) membrane proteins that are capable of maintaining high membrane curvature, thus helping shape the ER membrane into tubules. The mechanism of action of RTNs is hypothesized to be a combination of wedging, resulting from the transmembrane topology of their conserved reticulon homology domain, and scaffolding, arising from the ability of RTNs to form low-mobility homo-oligomers within the membrane. We studied the plant RTN isoform RTN13, which has previously been shown to locate to ER tubules and the edges of ER cisternae and to induce constrictions in ER tubules when overexpressed, and identified a region in the C terminus containing a putative amphipathic helix (APH). Here we show that deletion of this region or disruption of the hydrophobic face of the predicted helix abolishes the ability of RTN13 to induce constrictions of ER tubules in vivo. These mutants, however, still retain their ability to interact and form low-mobility oligomers in the ER membrane. Hence, our evidence indicates that the conserved APH is a key structural feature for RTN13 function in vivo, and we propose that RTN, like other membrane morphogens, rely on APHs for their function.
Item Type: | Journal Article | ||||||||||
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Subjects: | Q Science > QH Natural history | ||||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||||
Library of Congress Subject Headings (LCSH): | Endoplasmic reticulum | ||||||||||
Journal or Publication Title: | Proceedings of the National Academy of Sciences of the United States of America | ||||||||||
Publisher: | National Academy of Sciences | ||||||||||
ISSN: | 0027-8424 | ||||||||||
Official Date: | 27 September 2016 | ||||||||||
Dates: |
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Volume: | 113 | ||||||||||
Number: | 39 | ||||||||||
Page Range: | pp. 10902-10907 | ||||||||||
DOI: | 10.1073/pnas.1605434113 | ||||||||||
Status: | Peer Reviewed | ||||||||||
Publication Status: | Published | ||||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||||
Date of first compliant deposit: | 12 September 2016 | ||||||||||
Date of first compliant Open Access: | 27 October 2016 | ||||||||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) | ||||||||||
Grant number: | Grant PER ASPE | ||||||||||
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