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Yeast Aquaglyceroporins Use the Transmembrane Core to Restrict Glycerol Transport

Geijer, Cecilia; Ahmadpour, Doryaneh; Palmgren, Madelene; Filipsson, Caroline; Klein, Dagmara Medrala; Tamas, Markus J.; Hohmann, Stefan and Lindkvist, Karin LU (2012) In Journal of Biological Chemistry 287(28). p.23562-23570
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
287
issue
28
pages
23562 - 23570
publisher
ASBMB
external identifiers
  • wos:000306511300027
  • scopus:84863617765
ISSN
1083-351X
DOI
10.1074/jbc.M112.353482
language
English
LU publication?
yes
id
4d56da47-025b-49aa-bdb4-3a079574303d (old id 2991646)
date added to LUP
2012-09-03 07:17:07
date last changed
2017-08-27 03:08:58
@article{4d56da47-025b-49aa-bdb4-3a079574303d,
  abstract     = {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.},
  author       = {Geijer, Cecilia and Ahmadpour, Doryaneh and Palmgren, Madelene and Filipsson, Caroline and Klein, Dagmara Medrala and Tamas, Markus J. and Hohmann, Stefan and Lindkvist, Karin},
  issn         = {1083-351X},
  language     = {eng},
  number       = {28},
  pages        = {23562--23570},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Yeast Aquaglyceroporins Use the Transmembrane Core to Restrict Glycerol Transport},
  url          = {http://dx.doi.org/10.1074/jbc.M112.353482},
  volume       = {287},
  year         = {2012},
}