The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites
Abstract
Protein phosphorylation plays a key role in vasopressin signaling in the renal-collecting duct. Large-scale identification and quantification of phosphorylation events triggered by vasopressin is desirable to gain a comprehensive systems-level understanding of this process. We carried out phosphoproteomic analysis of rat inner medullary collecting duct cells by using a combination of phosphopeptide enrichment by immobilized metal affinity chromatography and phosphorylation site identification by liquid chromatography-mass spectrometry n neutral loss scanning. A total of 714 phosphorylation sites on 223 unique phosphoproteins were identified from inner medullary collecting duct samples treated short-term with either calyculin A or vasopressin. A number of proteins involved in cytoskeletal reorganization, vesicle trafficking, and transcriptional regulation were identified. Previously unidentified phosphorylation sites were found for membrane proteins essential to collecting duct physiology, including eight sites among aquaporin-2 (AQP2), aquaporin-4, and urea transporter isoforms A1 and A3. Through label-free quantification of phosphopeptides, we identified a number of proteins that significantly changed phosphorylation state in response to short-term vasopressin treatment: AQP2, Bclaf1, LRRC47, Rgl3, and SAFB2. In the presence of vasopressin, AQP2 monophosphorylated at S256 and diphosphorylated AQP2 (pS256/261) increased in abundance, whereas AQP2 monophosphorylated at S261 decreased, raising the possibility that both sites are involved in vasopressin-dependent AQP2 trafficking. This study reveals the practicality of liquid chromotography-mass spectrometry n neutral loss scanning for large-scale identification and quantification of protein phosphorylation in the analysis of cell signaling in a native mammalian system.
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Cites
Large-scale characterization of HeLa cell nuclear phosphoproteins
Beausoleil, S. A., Jedrychowski, M., Schwartz, D., Elias, J. E., Villén, J., Li, J., Cohn, M. A., Cantley, L. C., & Gygi, S. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404720101 · Cited by 1,375
Peri, S., Navarro, J. D., Amanchy, R., Kristiansen, T. Z., Jonnalagadda, C. K., Surendranath, V., Niranjan, V., Muthusamy, B., Gandhi, T. K. B., Gronborg, M., et al. (2003) · Genome Research · doi:10.1101/gr.1680803 · Cited by 1,089
Quantitative Phosphoproteomics Applied to the Yeast Pheromone Signaling Pathway
Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Færgeman, N. J., Mann, M., & Jensen, O. N. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400219-mcp200 · Cited by 763
Nühse, T. S., Stensballe, A., Jensen, O. N., & Peck, S. C. (2003) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t300006-mcp200 · Cited by 545
Inhibitory Phosphorylation Site for Rho-associated Kinase on Smooth Muscle Myosin Phosphatase
Feng, J., Ito, M., Ichikawa, K., Isaka, N., Nishikawa, M., Hartshorne, D. J., & Nakano, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37385 · Cited by 534
Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein
Neely, J. D., Amiry-Moghaddam, M., Ottersen, O. P., Froehner, S. C., Agre, P., & Adams, M. E. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241508198 · Cited by 488
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Phospho.ELM: A database of experimentally verified phosphorylation sites in eukaryotic proteins
Diella, F., Cameron, S., Gemünd, C., Linding, R., Via, A., Kuster, B., Sicheritz-Pontén, T., Blom, N., & Gibson, T. J. (2004) · BMC Bioinformatics · doi:10.1186/1471-2105-5-79 · Cited by 351
All in the family? New insights and questions regarding interconnectivity of Ras, Rap1 and Ral
Bos, J. L. (1998) · The EMBO Journal · doi:10.1093/emboj/17.23.6776 · Cited by 332
The pathobiology of the septin gene family
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Cited by
Large-scale proteomics and phosphoproteomics of urinary exosomes
Gonzales, P. A., Pisitkun, T., Hoffert, J. D., Tchapyjnikov, D., Star, R. A., Kleta, R., Wang, N. S., & Knepper, M. A. (2009) · Journal of the American Society of Nephrology · doi:10.1681/asn.2008040406 · Cited by 727
Self-citationThe Physiology of Urinary Concentration: An Update
Sands, J. M., & Layton, H. E. (2009) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2009.03.008 · Cited by 223
Lenoir, M., Ustunel, C., Rajesh, S., Kaur, J., Moreau, D., Gruenberg, J., & Overduin, M. (2018) · Nature Communications · doi:10.1038/s41467-018-03370-1 · Cited by 49
Signal integration and gene induction by a functionally distinct STAT3 phosphoform
Waitkus, M. S., Chandrasekharan, U. M., Willard, B., Tee, T. L., Hsieh, J. K., Przybycin, C. G., Rini, B. I., & DiCorleto, P. E. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00034-14 · Cited by 45
Metadata
- Authors
- Hoffert, J. D., Pisitkun, T., Wang, G., Shen, R.-F., & Knepper, M. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-05-02
- Volume
- 103
- Issue
- 18
- Pages
- 7159-7164
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2005126769
- Cited by
- 345
- References
- 35
- FWCI
- 9.95
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hoffert, J. D., Pisitkun, T., Wang, G., Shen, R.-F., & Knepper, M. A. (2006). Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0600895103
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