Protein secretion is initiated in the endoplasmic reticulum (ER) by capture of nascent proteins into COPII vesicles. Many proteins require cargo receptors to gain access to these vesicles. Cargo receptors cycle between the ER and Golgi, binding their clients in the ER and releasing them in the Golgi. We aim to understand the mechanisms that drive such context-specific interaction, and how client binding influences engagement with the vesicle formation machinery. The Miller lab has a long-standing expertise in vesicle formation and cargo selection, and largely uses yeast as a model system. We have in hand mutants that form the basis for this project, which will use a combination of genetics, biochemistry and structural biology to discover the mechanisms of selective and efficient ER export.

References

Silvere Pagant, Alexander Wu, Samuel Edwards, Frances Diehl, Elizabeth A Miller.  (2015)
Sec24 is a coincidence detector that simultaneously binds two signals to drive ER export.
Current Biology, 25(4):403-12.