Projects per year
Abstract / Description of output
NDR/LATS kinases regulate multiple aspects of cell polarity and morphogenesis from yeast to mammals. Fission yeast NDR/LATS kinase Orb6 has been proposed to control cell polarity by regulating the Cdc42 guanine nucleotide exchange factor Gef1. Here we show that Orb6 regulates polarity largely independently of Gef1 and that Orb6 positively regulates exocytosis. Through Orb6 inhibition in vivo and quantitative global phosphoproteomics, we identify Orb6 targets, including proteins involved in membrane trafficking. We confirm Sec3 and Sec5, conserved components of the exocyst complex, as substrates of Orb6 both in vivo and in vitro, and we show that Orb6 kinase activity is crucial for exocyst localization to actively-growing cell tips and for exocyst activity during septum dissolution after cytokinesis. We further show that Orb6 phosphorylation of Sec3 contributes to exocyst function in concert with exocyst protein Exo70. We propose that Orb6 contributes to polarized growth by regulating membrane trafficking at multiple levels.
Original language | English |
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Pages (from-to) | 1654-1667 |
Number of pages | 21 |
Journal | Cell Reports |
Volume | 26 |
Issue number | 6 |
DOIs | |
Publication status | Published - 5 Feb 2019 |
Keywords / Materials (for Non-textual outputs)
- Cdc42
- NDR/LATS kinase
- Orb6
- Schizosaccharomyces pombe
- Sec3
- exocyst
- exocytosis
- fission yeast
- phosphoproteomics
- phosphorylation
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Dive into the research topics of 'Fission yeast NDR/LATS kinase Orb6 regulates exocytosis via phosphorylation of exocyst complex'. Together they form a unique fingerprint.Projects
- 6 Finished
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Regulation of fission yeast cell polarity by stress-signalling pathways
1/09/18 → 31/08/23
Project: Research
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Profiles
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Andrew Goryachev
- School of Biological Sciences - Personal Chair in Computational Cell Biology
- Centre for Engineering Biology
Person: Academic: Research Active
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Kenneth Sawin
- School of Biological Sciences - Personal Chair in Cell Biology
Person: Academic: Research Active