دورية أكاديمية
Intracellular sites of AQP2 S256 phosphorylation identified using inhibitors of the AQP2 recycling itinerary.
| العنوان: | Intracellular sites of AQP2 S256 phosphorylation identified using inhibitors of the AQP2 recycling itinerary. |
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| المؤلفون: | Cheung PW; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Boukenna M; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Babicz RSE; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Mitra S; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Kay A; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Paunescu TC; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Baylor N; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Liu CS; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Nair AV; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Bouley R; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts., Brown D; Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts. |
| المصدر: | American journal of physiology. Renal physiology [Am J Physiol Renal Physiol] 2023 Feb 01; Vol. 324 (2), pp. F152-F167. Date of Electronic Publication: 2022 Dec 01. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Physiological Society Country of Publication: United States NLM ID: 100901990 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1522-1466 (Electronic) Linking ISSN: 15221466 NLM ISO Abbreviation: Am J Physiol Renal Physiol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Bethesda, Md. : American Physiological Society, c1997- |
| مواضيع طبية MeSH: | Aquaporin 2*/genetics , Aquaporin 2*/metabolism , Serine*/metabolism, Animals ; LLC-PK1 Cells ; Phosphorylation ; Swine ; Vasopressins/pharmacology ; Vasopressins/metabolism ; Intracellular Space/metabolism |
| مستخلص: | Vasopressin (VP)-regulated aquaporin-2 (AQP2) trafficking between cytoplasmic vesicles and the plasma membrane of kidney principal cells is essential for water homeostasis. VP affects AQP2 phosphorylation at several serine residues in the COOH-terminus; among them, serine 256 (S256) appears to be a major regulator of AQP2 trafficking. Mutation of this serine to aspartic acid, which mimics phosphorylation, induces constitutive membrane expression of AQP2. However, the intracellular location(s) at which S256 phosphorylation occurs remains elusive. Here, we used strategies to block AQP2 trafficking at different cellular locations in LLC-PK1 cells and monitored VP-stimulated phosphorylation of S256 at these sites by immunofluorescence and Western blot analysis with phospho-specific antibodies. Using methyl-β-cyclodextrin, cold block or bafilomycin, and taxol, we blocked AQP2 at the plasma membrane, in the perinuclear trans -Golgi network, and in scattered cytoplasmic vesicles, respectively. Regardless of its cellular location, VP induced a significant increase in S256 phosphorylation, and this effect was not dependent on a functional microtubule cytoskeleton. To further investigate whether protein kinase A (PKA) was responsible for S256 phosphorylation in these cellular compartments, we created PKA-null cells and blocked AQP2 trafficking using the same procedures. We found that S256 phosphorylation was no longer increased compared with baseline, regardless of AQP2 localization. Taken together, our data indicate that AQP2 S256 phosphorylation can occur at the plasma membrane, in the trans -Golgi network, or in cytoplasmic vesicles and that this event is dependent on the expression of PKA in these cells. NEW & NOTEWORTHY Phosphorylation of aquaporin-2 by PKA at serine 256 (S256) occurs in various subcellular locations during its recycling itinerary, suggesting that the protein complex necessary for AQP2 S256 phosphorylation is present in these different recycling stations. Furthermore, we showed, using PKA-null cells, that PKA activity is required for vasopressin-induced AQP2 phosphorylation. Our data reveal a complex spatial pattern of intracellular AQP2 phosphorylation at S256, shedding new light on the role of phosphorylation in AQP2 membrane accumulation. |
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| معلومات مُعتمدة: | S10 OD021577 United States OD NIH HHS; P30 DK043351 United States DK NIDDK NIH HHS; R25 DK101398 United States DK NIDDK NIH HHS; P30 DK057521 United States DK NIDDK NIH HHS; P30 DK135043 United States DK NIDDK NIH HHS; R01 DK096586 United States DK NIDDK NIH HHS; S10 RR031563 United States RR NCRR NIH HHS; K08 DK115901 United States DK NIDDK NIH HHS; T32 DK007540 United States DK NIDDK NIH HHS |
| فهرسة مساهمة: | Keywords: aquaporin 2; exocytosis; protein kinase A; vesicle recycling; water channel |
| المشرفين على المادة: | 0 (Aquaporin 2) 452VLY9402 (Serine) 11000-17-2 (Vasopressins) |
| تواريخ الأحداث: | Date Created: 20221201 Date Completed: 20230123 Latest Revision: 20240228 |
| رمز التحديث: | 20240228 |
| مُعرف محوري في PubMed: | PMC9844975 |
| DOI: | 10.1152/ajprenal.00123.2022 |
| PMID: | 36454701 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1522-1466 |
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| DOI: | 10.1152/ajprenal.00123.2022 |