Phosphatidylinositol (3,5) bisphosphate dependent membrane trafficking in S. cerevisiae

Williams, Fay Kathleen (2012). Phosphatidylinositol (3,5) bisphosphate dependent membrane trafficking in S. cerevisiae. University of Birmingham. Ph.D.

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Abstract

Phosphoinositides are lipid signals that control cellular processes and are particularly closely associated with the control of membrane trafficking. PtdIns(3,5) \(\char{cmmi10}{0x50}\)\(_2\) is the most recently identified phosphoinositide and was previously recognised as controlling events in the late endocytic system between the late endosome and the vacuole/lysosome. Primarily associated with retrograde trafficking from the vacuole/lysosome to the late endosome/MVB, PtdIns(3,5) \(\char{cmmi10}{0x50}\)\(_2\) is generated by the kinase Fab1p (PIKfyve in animals). In mammalian cells, PtdIns(3,5) \(\char{cmmi10}{0x50}\)\(_2\) has also been implicated in control of ill-defined trafficking pathways close to the Golgi; for example, the recycling of mannose-6-phosphate receptor (M6R) back to the Golgi and also the trafficking of some types of ion and nutrient channels from the Golgi to the cell surface. This thesis describes attempts to study putative PtdIns(3,5) \(\char{cmmi10}{0x50}\)\(_2\) dependent trafficking in the early endocytic system of \(\char{cmmi10}{0x53}\). \(\char{cmmi10}{0x63}\)\(\char{cmmi10}{0x65}\)\(\char{cmmi10}{0x72}\)\(\char{cmmi10}{0x65}\)\(\char{cmmi10}{0x76}\)\(\char{cmmi10}{0x69}\)\(\char{cmmi10}{0x73}\)\(\char{cmmi10}{0x69}\)\(\char{cmmi10}{0x61}\)\(\char{cmmi10}{0x65}\) using two model proteins; the recycling of Vps10p from late endosome to Golgi and of Chs3p from recycling endosome to Golgi.

Type of Work: Thesis (Doctorates > Ph.D.)
Award Type: Doctorates > Ph.D.
Supervisor(s):
Supervisor(s)EmailORCID
Dove, Stephen K.UNSPECIFIEDUNSPECIFIED
Mitchell, Robert H.UNSPECIFIEDUNSPECIFIED
Licence:
College/Faculty: Colleges (2008 onwards) > College of Life & Environmental Sciences
School or Department: School of Biosciences
Funders: Other
Other Funders: The University of Birmingham, The University of Birmingham
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
URI: http://etheses.bham.ac.uk/id/eprint/3626

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