Aquaporin‐mediated water transport across cellular membranes is an ancient, ubiquitous mechanism within cell biology. This family of integral membrane proteins includes both water selective pores (aquaporins) and transport facilitators of other small molecules such as glycerol and urea (aquaglyceroporins). Eukaryotic aquaporins are frequently regulated post‐translationally by gating, whereby the rate of flux through the channel is controlled, or by trafficking, whereby aquaporins are shuttled from intracellular storage sites to the plasma membrane. A number of high‐resolution X‐ray structures of eukaryotic aquaporins have recently been reported and the new structural insights into gating and trafficking that emerged from these studies are described. Basic structural themes reoccur, illustrating how the problem of regulation in diverse biological contexts builds upon a limited set of possible solutions.
Structural insights into eukaryotic aquaporin regulation
S. Törnroth-Horsefield,Kristina Hedfalk,G. Fischer,K. Lindkvist-Petersson,R. Neutze
Published 2010 in FEBS Letters
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- Publication year
2010
- Venue
FEBS Letters
- Publication date
2010-06-18
- Fields of study
Biology, Medicine
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Semantic Scholar, PubMed
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