The yeast proteolipid Pmp3p is a new component of the plasma membrane microdomains associated with the eisosomes
(2010)
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- Authors
- Supervisors
- Morsomme, Pierre
- Abstract
- (en) Many prokaryotic and eukaryotic organisms possess small molecular weight hydrophobic proteins that respond differently to stresses, such as cold temperature, salt and dehydration. Yeast plasma membranes contain a small 55 amino acid hydrophobic polypeptide, Pmp3p/Sna1p, which belongs to the SNA (Sensitive to Na) proteins family and has three close homologues, called Sna2p, Sna3p and Sna4p. Previous work showed that the PMP3 deletion increases the plasma membrane potential and confers sensitivity to cytotoxic cations. In this study we present a further characterization of the molecular function of Pmp3p. We observed that Pmp3p physically interacts with Pil1p, a component of the eisosomes which are structures associated with some plasma membrane microdomains. We confirmed the localization of Pmp3p in these microdomains via indirect immunofluorescence. Using different techniques in molecular biology, biochemistry, cell biology and proteomics, we showed that Pmp3p could protect some transporters against endocytosis and link this process to cation homeostasis. Finally, a site-directed mutagenesis approach revealed that at least 9 conserved residues (F14, P17, G25, D29, L36, L39, P43, A48, Y50) are important for the function of Pmp3p.
- Affiliations
Citations
Hochstenbach, J.-F. (2010). The yeast proteolipid Pmp3p is a new component of the plasma membrane microdomains associated with the eisosomes. https://hdl.handle.net/2078.5/130157