HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 4, 2975-2983, January 23, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/4/2975    most recent M310767200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hendriks, G. Articles by van der Sluijs, P. Search for Related Content PubMed PubMed Citation Articles by Hendriks, G. Articles by van der Sluijs, P. Social Bookmarking                      What's this?

Glycosylation Is Important for Cell Surface Expression of the Water Channel Aquaporin-2 but Is Not Essential for Tetramerization in the Endoplasmic Reticulum^*

Giel Hendriks, Marco Koudijs, Bas W. M. van Balkom, Viola Oorschot, Judith Klumperman, Peter M. T. Deen, and Peter van der Sluijs

From the Department of Cell Biology, University Medical Center Utrecht, Utrecht 3584 CX and the Department of Physiology, University Medical Center, Nijmegen 6500 HB, The Netherlands

Aquaporin-2 (AQP2) is a pore-forming protein that is required for regulated reabsorption of water from urine. Mutations in AQP2 lead to nephrogenic diabetes insipidus, a disorder in which functional AQP2 is not expressed on the apical cell surface of kidney collecting duct principal cells. The mechanisms and pathways directing AQP2 from the endoplasmic reticulum to the Golgi complex and beyond have not been defined. We found that 25% of newly synthesized AQP2 is glycosylated. Nonglycosylated and complex-glycosylated wild-type AQP2 are stable proteins with a half-life of 6-12 h and are both detectable on the cell surface. We show that AQP2 forms tetramers in the endoplasmic reticulum during or very early after synthesis and reaches the Golgi complex in 1-1.5 h. We also report that glycosylation is neither essential for tetramerization nor for transport from the endoplasmic reticulum to the Golgi complex. Instead, the N-linked glycan is important for exit from the Golgi complex and sorting of AQP2 to the plasma membrane. These results are important for understanding the molecular mechanisms responsible for the intracellular retention of AQP2 in nephrogenic diabetes insipidus.

Received for publication, September 30, 2003 , and in revised form, October 30, 2003.

^* This work was supported by The Netherlands Organization for Medical Research (to P. v. d. S. and P. M. T. D.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Cell Biology, University Medical Center Utrecht, AZU Rm. G02.525, Heidelberglaan 100, Utrecht 3584 CX, The Netherlands. Tel.: 31-30-250-7574; Fax: 31-30-254-1797; E-mail: pvander{at}knoware.nl

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				X.-b. Chang, A. Mengos, Y.-x. Hou, L. Cui, T. J. Jensen, A. Aleksandrov, J. R. Riordan, and M. Gentzsch Role of N-linked oligosaccharides in the biosynthetic processing of the cystic fibrosis membrane conductance regulator J. Cell Sci., September 1, 2008; 121(17): 2814 - 2823. [Abstract] [Full Text] [PDF]

				S. Budik, I. Walter, W. Tschulenk, M. Helmreich, K. Deichsel, F. Pittner, and C. Aurich Significance of aquaporins and sodium potassium ATPase subunits for expansion of the early equine conceptus Reproduction, April 1, 2008; 135(4): 497 - 508. [Abstract] [Full Text] [PDF]

				G. Akabane, Y. Ogushi, T. Hasegawa, M. Suzuki, and S. Tanaka Gene cloning and expression of an aquaporin (AQP-h3BL) in the basolateral membrane of water-permeable epithelial cells in osmoregulatory organs of the tree frog Am J Physiol Regulatory Integrative Comp Physiol, June 1, 2007; 292(6): R2340 - R2351. [Abstract] [Full Text] [PDF]

				I. Erler, D. M. M. Al-Ansary, U. Wissenbach, T. F. J. Wagner, V. Flockerzi, and B. A. Niemeyer Trafficking and Assembly of the Cold-sensitive TRPM8 Channel J. Biol. Chem., December 15, 2006; 281(50): 38396 - 38404. [Abstract] [Full Text] [PDF]

				E.-J. Kamsteeg, G. Hendriks, M. Boone, I. B. M. Konings, V. Oorschot, P. van der Sluijs, J. Klumperman, and P. M. T. Deen Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channel PNAS, November 28, 2006; 103(48): 18344 - 18349. [Abstract] [Full Text] [PDF]

				G. Chen, O. Frohlich, Y. Yang, J. D. Klein, and J. M. Sands Loss of N-Linked Glycosylation Reduces Urea Transporter UT-A1 Response to Vasopressin J. Biol. Chem., September 15, 2006; 281(37): 27436 - 27442. [Abstract] [Full Text] [PDF]

				D. Spasic, A. Tolia, K. Dillen, V. Baert, B. De Strooper, S. Vrijens, and W. Annaert Presenilin-1 Maintains a Nine-Transmembrane Topology throughout the Secretory Pathway J. Biol. Chem., September 8, 2006; 281(36): 26569 - 26577. [Abstract] [Full Text] [PDF]

				F. J. M. Detmers, B. L. de Groot, E. M. Muller, A. Hinton, I. B. M. Konings, M. Sze, S. L. Flitsch, H. Grubmuller, and P. M. T. Deen Quaternary Ammonium Compounds as Water Channel Blockers: SPECIFICITY, POTENCY, AND SITE OF ACTION J. Biol. Chem., May 19, 2006; 281(20): 14207 - 14214. [Abstract] [Full Text] [PDF]

				F. de Mattia, P. J.M. Savelkoul, D. G. Bichet, E.-J. Kamsteeg, I. B.M. Konings, N. Marr, M.-F. Arthus, M. Lonergan, C. H. van Os, P. van der Sluijs, et al. A novel mechanism in recessive nephrogenic diabetes insipidus: wild-type aquaporin-2 rescues the apical membrane expression of intracellularly retained AQP2-P262L Hum. Mol. Genet., December 15, 2004; 13(24): 3045 - 3056. [Abstract] [Full Text] [PDF]

				O. Vagin, S. Turdikulova, and G. Sachs The H,K-ATPase {beta} Subunit as a Model to Study the Role of N-Glycosylation in Membrane Trafficking and Apical Sorting J. Biol. Chem., September 10, 2004; 279(37): 39026 - 39034. [Abstract] [Full Text] [PDF]