2010
DOI: 10.1111/j.1600-0854.2010.01134.x
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Reticulon Short Hairpin Transmembrane Domains Are Used to Shape ER Tubules

Abstract: Reticulons are integral membrane proteins that partition into and shape the tubular endoplasmic reticulum (ER). We propose that reticulons use a membrane insertion mechanism to generate regions of high membrane curvature in the ER. A reticulon contains two short hairpin transmembrane domains (TMDs), which could generate membrane curvature by increasing the area of the cytoplasmic leaflet. Here, we test whether the short length of these hairpin TMDs is required for reticulon membrane-shaping functions in mammal… Show more

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Cited by 195 publications
(205 citation statements)
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“…However, the energetic costs of exposing peptide bonds to the acyl chains (47) likely favor local rearrangements of the lipid bilayer, as observed with model transmembrane peptides (48). Effectively short transmembrane domains may play a role in RHD localization, because highly curved membranes are expected to be significantly thinner (49), and may explain why lengthening the transmembrane regions of RHDs results in defective localization (20,21).…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…However, the energetic costs of exposing peptide bonds to the acyl chains (47) likely favor local rearrangements of the lipid bilayer, as observed with model transmembrane peptides (48). Effectively short transmembrane domains may play a role in RHD localization, because highly curved membranes are expected to be significantly thinner (49), and may explain why lengthening the transmembrane regions of RHDs results in defective localization (20,21).…”
Section: Discussionmentioning
confidence: 99%
“…However, there is currently no structural information available for these intramembrane domains, and the exact mechanism of curvature generation and stabilization remains unknown. The mechanism for exclusive localization of RHD proteins to highly curved membranes also remains unclear; however, the transmembrane domains have been implicated in both membrane localization and curvature stabilization (4,20,21).Yop1p is one of the best characterized of the RHD-containing proteins (4, 5). It is a member of the DP1 family and has the highest functional and sequence conservation with human REEP5 (19).…”
mentioning
confidence: 99%
“…The members of this diverse family of proteins share a common protein motif called the reticulon homology domain (RHD). The hydrophobic ∌200-amino-acid RHD likely forms a helical hairpin structure that intercalates four hydrophobic helical segments into the outer leaflet of the ER membrane to induce curvature and maintain a tubular shape Zurek et al, 2011). Many members of the Reticulon, REEP and DP1 family also contain an extended N-terminal segment ranging from a few hundred to a thousand amino acids that likely provides additional functionality (Di Sano et al, 2012).…”
Section: Introductionmentioning
confidence: 99%
“…Cytb5-EGFP was kindly provided by Claudio Hetz (Universidad de Chile, Chile). BFP-Sec61b (ER-BFP), ARF1-Q71I-HA and Sar1-H79G-HA have been described previously (Ward et al, 2001;Jeyifous et al, 2009;Zurek et al, 2011). Kif5CDN-RFP corresponds to amino acids 678-955 of KIF5C (accession number NM_001107730).…”
Section: Cellsmentioning
confidence: 99%
“…We first carried out live-cell imaging to characterize the dynamic relationship between intracellular GABA B1 and the ER in the soma and dendrites of neurons cotransfected with GABA B1 -mRFP or GABA B1 -EGFP and ER-BFP, a vector that encodes a blue fluorescent protein fused to the human ER resident protein Sec61b -the encoded fusion protein strongly labels the ER (Zurek et al, 2011). Although the spatial resolution was not sufficient to visualize the tubular network because of its densely packed nature (Spacek and Harris, 1997), punctate and irregular structures containing fluorescent GABA B1 were observed in the somatic and dendritic compartments, and their distribution patterns changed over time ( Fig.…”
Section: Gaba B1 Transports Within the Ermentioning
confidence: 99%