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Title: A molecular analysis of endosome to plasma membrane recycling mediated by retromer
Author: Gallon , Matthew
ISNI:       0000 0004 5923 8152
Awarding Body: University of Bristol
Current Institution: University of Bristol
Date of Award: 2015
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The endosomal network is a crucial hub in the trafficking of proteins through the cellular endomembrane system. Cargo proteins enter endosomes by endocytosis from the plasma or by trafficking from the trans-Golgi network (TGN). Here, cargo proteins face one of two fates: retention in the endosome, leading ultimately to lysosomal degradation, or export from the endosome for re-use ("recycling"). The balance of protein degradation and recycling is crucial to cellular homeostasis; inappropriate sorting of proteins to either fate leads to cellular dysfunction. Retromer is an endosome-membrane-associated protein complex central to the recycling of many cargo proteins from endosomes, both to the TGN and the plasma membrane. Retromer function is reliant on a number of proteins from the sorting nexin (SNX) family, one of which is SNX27. SNX27 is unique among SNXs in its bearing a POZ domain that binds POZ binding motifs (PDZbms) in the cytoplasmic tails of trans-membrane cargo proteins. SNX27 is required for retromer-mediated endosome-plasma-membrane recycling of POZbm-containing cargo proteins. In this thesis I firstly investigate the role of SNX27 in the trafficking of transmembrane proteins that control planar cell polarity. I next show that SNX27 interacts directly with retromer and dissect the molecular details of this interaction. I then identify other proteins that interact with retromer using SILAC-based proteomics and investigate three of the proteins identified in greater detail. Overall, these data add to the growing appreciation of retromer as a master regulator of endosomal recycling.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available