Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5
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Title
Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 292, Issue 35, Pages 14636-14648
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2017-07-15
DOI
10.1074/jbc.m117.788364
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Note: Only part of the references are listed.- The Aquaporin Splice Variant NbXIP1;1α Is Permeable to Boric Acid and Is Phosphorylated in the N-terminal Domain
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- Collecting Duct Principal Cell Transport Processes and Their Regulation
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- Highly sensitive detection of protein phosphorylation by using improved Phos-tag Biotin
- (2012) Eiji Kinoshita et al. PROTEOMICS
- Regulation of AQP2 localization by S256 and S261 phosphorylation and ubiquitination
- (2010) Grazia Tamma et al. AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
- Structural Role of the Vps4-Vta1 Interface in ESCRT-III Recycling
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- Detergent binding explains anomalous SDS-PAGE migration of membrane proteins
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- Vasopressin-stimulated Increase in Phosphorylation at Ser269Potentiates Plasma Membrane Retention of Aquaporin-2
- (2008) Jason D. Hoffert et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Coordinated protein sorting, targeting and distribution in polarized cells
- (2008) Ira Mellman et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
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- Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin
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