Journal
JOURNAL OF CELL SCIENCE
Volume 133, Issue 19, Pages -Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.250100
Keywords
Membrane transport; Structural Biology; Trafficking receptors
Categories
Funding
- Wellcome Trust [219531/Z/19/Z, 215519/Z/19/Z]
- University of Oxford
- Wellcome Trust [215519/Z/19/Z, 219531/Z/19/Z] Funding Source: Wellcome Trust
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Protein localisation in the cell is controlled through the function of trafficking receptors, which recognise specific signal sequences and direct cargo proteins to different locations. The KDEL receptor (KDELR) was one of the first intracellular trafficking receptors identified and plays an essential role in maintaining the integrity of the early secretory pathway. The receptor recognises variants of a canonical C-terminal Lys-Asp-Glu-Leu (KDEL) signal sequence on ER-resident proteins when these escape to the Golgi, and targets these proteins to COPI-coated vesicles for retrograde transport back to the ER. The empty receptor is then recycled from the ER back to the Golgi by COPII-coated vesicles. Crystal structures of the KDELR show that it is structurally related to the PQ-loop family of transporters that are found in both pro- and eukaryotes, and shuttle sugars, amino acids and vitamins across cellular membranes. Furthermore, analogous to PQ-loop transporters, the KDELR undergoes a pH-dependent and ligand-regulated conformational cycle. Here, we propose that the striking structural similarity between the KDELR and PQ-loop transporters reveals a connection between transport and trafficking in the cell, with important implications for understanding trafficking receptor evolution and function.
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