NDLI: Annexin A2 Mediates Apical Trafficking of Renal $Na^{+}-K^{+}-2Cl^{−}$ Cotransporter

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Annexin A2 Mediates Apical Trafficking of Renal $Na^{+}-K^{+}-2Cl^{−}$ Cotransporter

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Annexin A2 Mediates Apical Trafficking of Renal $Na^{+}-K^{+}-2Cl^{−}$ Cotransporter

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Daigeler, Anna-lena Kalis, Ronny Seifert, Wenke Paliege, Alexander Mrowka, Ralf Dathe, Christin Mutig, Kerim Wanker, Erich Jankowski, Vera Bachmann, Sebastian
Description	Author Affiliation: Dathe C ( From the Department of Anatomy, Charité-Universitätsmedizin Berlin, 10115 Berlin.)
Abstract	The furosemide-sensitive Na(+)-K(+)-2Cl(-) cotransporter (NKCC2) is responsible for urine concentration and helps maintain systemic salt homeostasis. Its activity depends on trafficking to, and insertion into, the apical membrane, as well as on phosphorylation of conserved N-terminal serine and threonine residues. Vasopressin (AVP) signaling via PKA and other kinases activates NKCC2. Association of NKCC2 with lipid rafts facilitates its AVP-induced apical translocation and activation at the surface. Lipid raft microdomains typically serve as platforms for membrane proteins to facilitate their interactions with other proteins, but little is known about partners that interact with NKCC2. Yeast two-hybrid screening identified an interaction between NKCC2 and the cytosolic protein, annexin A2 (AnxA2). Annexins mediate lipid raft-dependent trafficking of transmembrane proteins, including the AVP-regulated water channel, aquaporin 2. Here, we demonstrate that AnxA2, which binds to phospholipids in a Ca(2+)-dependent manner and may organize microdomains, is codistributed with NKCC2 to promote its apical translocation in response to AVP stimulation and low chloride hypotonic stress. NKCC2 and AnxA2 interact in a phosphorylation-dependent manner. Phosphomimetic AnxA2 carrying a mutant phosphoacceptor (AnxA2-Y24D-GFP) enhanced surface expression and raft association of NKCC2 by 5-fold upon low chloride hypotonic stimulation, whereas AnxA2-Y24A-GFP and PKC-dependent AnxA2-S26D-GFP did not. As the AnxA2 effect involved only nonphosphorylated NKCC2, it appears to affect NKCC2 trafficking. Overexpression or knockdown experiments further supported the role of AnxA2 in the apical translocation and surface expression of NKCC2. In summary, this study identifies AnxA2 as a lipid raft-associated trafficking factor for NKCC2 and provides mechanistic insight into the regulation of this essential cotransporter.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	14
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-04-04
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Annexin A2 Metabolism Membrane Microdomains Solute Carrier Family 12, Member 1 Amino Acid Substitution Animals Genetics Antidiuretic Agents Pharmacology HEK293 Cells Macaca Mulatta Mutation, Missense Phosphorylation Drug Effects Protein Transport Rats, Sprague-Dawley Vasopressins Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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