Lipid phosphate phosphatases dimerise,but this interaction is not required for <Emphasis Type="Italic">in vivo</Emphasis> activity |
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| Authors: | Camilla?Burnett Panagiota?Makridou Lindsay?Hewlett Email author" target="_blank">Ken?HowardEmail author |
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| Institution: | (1) Department of Physiology, MRC Laboratory for Molecular Cell Biology, University College London, Gower St, London, WC1E 6BT, UK |
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| Abstract: | Background Lipid phosphate phosphatases (LPPs) are integral membrane proteins believed to dephosphorylate bioactive lipid messengers,
so modifying or attenuating their activities. Wunen, a Drosophila LPP homologue, has been shown to play a pivotal role in
primordial germ cell (PGC) migration and survival during embryogenesis. It has been hypothesised that LPPs may form oligomeric
complexes, and may even function as hexamers. We were interested in exploring this possibility, to confirm whether LPPs can
oligomerise, and if they do, whether oligomerisation is required for either in vitroor in vivoactivity. |
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