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Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5

  • Published:2017-09 Issue:35 Volume:292 Page:14636-14648
  • ISSN:0021-9258
  • Container-title:Journal of Biological Chemistry
  • language:en
  • Short-container-title:Journal of Biological Chemistry

Author:

Roche Jennifer Virginia,Survery Sabeen,Kreida Stefan,Nesverova Veronika,Ampah-Korsah Henry,Gourdon Maria,Deen Peter M.T.,Törnroth-Horsefield Susanna

Funder

Vetenskapsrådet

Crafoordska Stiftelsen

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference37 articles.

1. Collecting duct principal cell transport processes and their regulation;Pearce;Clin. J. Am. Soc. Nephrol,2015

2. Phosphorylation of serine 256 is required for cAMP-dependent regulatory exocytosis of the aquaporin-2 water channel;Fushimi;J. Biol. Chem,1997

3. Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells;Katsura;Am. J. Physiol,1997

4. The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel;van Balkom;J. Biol. Chem,2002

5. Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channel;Kamsteeg;Proc. Natl. Acad. Sci. U.S.A,2006

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