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The integral membrane proteins of the DP1 (deleted in polyposis) and reticulon families are responsible for maintaining the high membrane curvature required for both smooth endoplasmic reticulum (ER) tubules and the edges of ER sheets, and mutations in these proteins lead to motor neuron diseases, such as hereditary spastic paraplegia. Reticulon/DP1 proteins contain reticulon homology domains (RHDs) that have unusually long hydrophobic segments and are proposed to adopt intramembrane helical hairpins that stabilize membrane curvature. We have characterized the secondary structure and dynamics of the DP1 family protein produced from the YOP1 gene (Yop1p) and identified a C-terminal conserved amphipathic helix (APH) that, on its own, interacts strongly with negatively charged membranes and is necessary for membrane tubule formation. Analyses of DP1 and reticulon family members indicate that most, if not all, contain C-terminal sequences capable of forming APHs. Together, these results indicate that APHs play a previously unrecognized role in RHD membrane curvature stabilization.

Original publication

DOI

10.1073/pnas.1415882112

Type

Journal article

Journal

Proc Natl Acad Sci U S A

Publication Date

17/02/2015

Volume

112

Pages

E639 - E648

Keywords

DP1, Yop1p, amphipathic helix, reticulon, tubular ER, Biopolymers, Cell Membrane, Electrophoresis, Polyacrylamide Gel, Escherichia coli Proteins, Micelles, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary