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Yeast Aquaglyceroporins Use the Transmembrane Core to Restrict Glycerol Transport

Artikel i vetenskaplig tidskrift
Författare Cecilia Geijer
Doryaneh Ahmadpour
Madelene Palmgren
Caroline Filipsson
Dagmara Medrala Klein
Markus J. Tamás
Stefan Hohmann
Karin Lindkvist-Petersson
Publicerad i Journal of Biological Chemistry
Volym 287
Nummer/häfte 28
Sidor 23562-23570
ISSN 0021-9258
Publiceringsår 2012
Publicerad vid Institutionen för kemi och molekylärbiologi
Sidor 23562-23570
Språk en
Länkar dx.doi.org/10.1074/jbc.M112.353482
Ämnesord fungus ashbya-gossypii, regulatory domain, osmotic-stress, channel, fps1p, protein, selectivity, aquaporin, facilitator, mechanism, membrane, eston gm, 1991, proceedings of the national academy of sciences of the united states
Ämneskategorier Biokemi och molekylärbiologi

Sammanfattning

Aquaglyceroporins are transmembrane proteins belonging to the family of aquaporins, which facilitate the passage of specific uncharged solutes across membranes of cells. The yeast aquaglyceroporin Fps1 is important for osmoadaptation by regulating intracellular glycerol levels during changes in external osmolarity. Upon high osmolarity conditions, yeast accumulates glycerol by increased production of the osmolyte and by restricting glycerol efflux through Fps1. The extended cytosolic termini of Fps1 contain short domains that are important for regulating glycerol flux through the channel. Here we show that the transmembrane core of the protein plays an equally important role. The evidence is based on results from an intragenic suppressor mutation screen and domain swapping between the regulated variant of Fps1 from Saccharomyces cerevisiae and the hyperactive Fps1 ortholog from Ashbya gossypii. This suggests a novel mechanism for regulation of glycerol flux in yeast, where the termini alone are not sufficient to restrict Fps1 transport. We propose that glycerol flux through the channel is regulated by interplay between the transmembrane helices and the termini. This mechanism enables yeast cells to fine-tune intracellular glycerol levels at a wide range of extracellular osmolarities.

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