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Title: Function and regulation of the WASH complex in the endocytic cycle
Author: Park, Laura
ISNI:       0000 0004 2736 3784
Awarding Body: University of Glasgow
Current Institution: University of Glasgow
Date of Award: 2012
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The WASH complex is highly conserved and consists of the actin nucleation promoter, WASH, and several regulatory subunits; Strumpellin, SWIP, ccdc53 and FAM21. Previously, it has been shown that WASH directs construction of actin coats on lysosomes. This actin coat is required for removal of V-ATPase complexes from lysosomal membranes, allowing neutralization and maturation to post-lysosomes. WASH null cells are blocked at the acidic lysosome stage and are thus unable to perform exocytosis. We now show that FAM21 acts at a different step in the same pathway. FAM21 nulls are still blocked in exocytosis, but the remaining complex is functional in removal of V-ATPase, allowing progression to post-lysosome. We hypothesize that the role of FAM21 is to release the WASH complex from post-lysosome membranes in order to allow recycling back to newly formed acidic lysosomes. We have also shown that capping protein interacts with the WASH complex through FAM21, and this interaction is essential for progression to exocytosis, likely contributing to the mechanism by which FAM21 regulates and releases the WASH complex from post-lysosomal membranes.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available
Keywords: Q Science (General)