Regulation of the water channel aquaporin-2 by posttranslational modification

The cellular functions of many eukaryotic membrane proteins, including the vasopressin-regulated water channel aquaporin-2 (AQP2), are regulated by posttranslational modifications. In this article, we discuss the experimental discoveries that have advanced our understanding of how posttranslational...

Full description

Saved in:
Bibliographic Details
Published in:American journal of physiology. Renal physiology 2011-05, Vol.300 (5), p.F1062-F1073
Main Authors: Moeller, Hanne B, Olesen, Emma T B, Fenton, Robert A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Aquaporin 2 - metabolism
Diabetes
Endocytosis
Eukaryotes
Exocytosis
Glycosylation
Humans
Ion Channel Gating
Kidney - metabolism
Kidney diseases
Membranes
Molecular Sequence Data
Phosphorylation
Protein Kinases - metabolism
Protein Processing, Post-Translational
Protein Transport
Proteins
Ubiquitination
Water - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The cellular functions of many eukaryotic membrane proteins, including the vasopressin-regulated water channel aquaporin-2 (AQP2), are regulated by posttranslational modifications. In this article, we discuss the experimental discoveries that have advanced our understanding of how posttranslational modifications affect AQP2 function, especially as they relate to the role of AQP2 in the kidney. We review the most recent data demonstrating that glycosylation and, in particular, phosphorylation and ubiquitination are mechanisms that regulate AQP2 activity, subcellular sorting and distribution, degradation, and protein interactions. From a clinical perspective, posttranslational modification resulting in protein misrouting or degradation may explain certain forms of nephrogenic diabetes insipidus. In addition to providing major insight into the function and dynamics of renal AQP2 regulation, the analysis of AQP2 posttranslational modification may provide general clues as to the role of posttranslational modification for regulation of other membrane proteins.
ISSN:1931-857X
1522-1466
DOI:10.1152/ajprenal.00721.2010