Steric exclusion and protein conformation determine the localization of plasma membrane transporters

Frans Bianchi, Łukasz Syga, Gemma Moiset, Dian Spakman, Paul E. Schavemaker, Christiaan M. Punter, Anne-Bart Seinen, Antoine M. Oijen, Andrew Robinson and Bert Poolman ()
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Frans Bianchi: University of Groningen
Łukasz Syga: University of Groningen
Gemma Moiset: University of Groningen
Dian Spakman: University of Groningen
Paul E. Schavemaker: University of Groningen
Christiaan M. Punter: University of Groningen
Anne-Bart Seinen: University of Groningen
Antoine M. Oijen: Zernike Institute for Advanced Materials
Andrew Robinson: Zernike Institute for Advanced Materials
Bert Poolman: University of Groningen

Nature Communications, 2018, vol. 9, issue 1, 1-13

Abstract: Abstract The plasma membrane (PM) of Saccharomyces cerevisiae contains membrane compartments, MCC/eisosomes and MCPs, named after the protein residents Can1 and Pma1, respectively. Using high-resolution fluorescence microscopy techniques we show that Can1 and the homologous transporter Lyp1 are able to diffuse into the MCC/eisosomes, where a limited number of proteins are conditionally trapped at the (outer) edge of the compartment. Upon addition of substrate, the immobilized proteins diffuse away from the MCC/eisosomes, presumably after taking a different conformation in the substrate-bound state. Our data indicate that the mobile fraction of all integral plasma membrane proteins tested shows extremely slow Brownian diffusion through most of the PM. We also show that proteins with large cytoplasmic domains, such as Pma1 and synthetic chimera of Can1 and Lyp1, are excluded from the MCC/eisosomes. We hypothesize that the distinct localization patterns found for these integral membrane proteins in S. cerevisiae arises from a combination of slow lateral diffusion, steric exclusion, and conditional trapping in membrane compartments.

Date: 2018
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DOI: 10.1038/s41467-018-02864-2

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