How are individual transmembrane helices in polytopic membrane proteins delivered from the Sec translocon into the lipid bilayer? A new study on the aquaporin-4 water channel shows that they move out of the translocon in succession but may linger nearby for an extended period of time.
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References
Sadlish, H., Pitonzo, D., Johnson, A.E. & Skach, W.R. Nat. Struct. Mol. Biol. 12, 870–878 (2005).
Rapoport, T.A., Goder, V., Heinrich, S.U. & Matlack, K.E. Trends Cell Biol. 14, 568–575 (2004).
Alder, N.N. & Johnson, A.E. J. Biol. Chem. 279, 22787–22790 (2004).
van den Berg, B. et al. Nature 427, 36–44 (2004).
Heinrich, S., Mothes, W., Brunner, J. & Rapoport, T. Cell 102, 233–244 (2000).
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Heijne, G. Helices on the move. Nat Struct Mol Biol 12, 834–835 (2005). https://doi.org/10.1038/nsmb1005-834
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DOI: https://doi.org/10.1038/nsmb1005-834