Cells face a complex problem: how to transfer lipids and proteins between membrane compartments in an organized, timely fashion. Indeed, many thousands of membrane and secretory proteins must traffic out of the ER to different organelles to function, while others are retrieved from the plasma membrane having fulfilled their roles [Nat. Rev. Mol. Cell Biol. (2013) 14, 382–392]. This process is highly dynamic and failure to target cargo accurately leads to catastrophic consequences for the cell, as is clear from the numerous human diseases associated with defects in membrane trafficking [Int. J. Mol. Sci. (2013) 14, 18670–18681; Traffic (2000) 1, 836–851]. How then does the cell organize this enormous transfer of material in its crowded internal environment? And how specifically do vesicles carrying proteins and lipids recognize and fuse with the correct compartment?
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February 2018
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Cover Image
Cover Image
In this issue of Biochemical Society Transactions, Elliott and Jones review some of the techniques used to prepare, measure and analyse the electron transfer properties of metalloproteins, concentrating on scanning tunnelling microscopy-based techniques and advances in attachment of proteins to electrodes. The cover image, taken from Figure 2 in the review, shows the direct attachment of a protein (cytochrome b562) to gold substrate through an engineered cysteine residue. For further information see pages 1–9.
Review Article|
December 22 2017
At the ends of their tethers! How coiled-coil proteins capture vesicles at the Golgi
Biochem Soc Trans (2018) 46 (1): 43–50.
Article history
Received:
October 17 2017
Revision Received:
November 22 2017
Accepted:
November 23 2017
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