Structural and functional analysis of the transmembrane segment pair VI and VII of the NHE1 isoform of the Na+/H+ exchanger

Biochemistry

Volumn 53, Issue 22, 2014, Pages 3658-3670

  Alves, Claudia ^a   Lee, Brian L ^a   Sykes, Brian D ^a   Fliegel, Larry ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; AMINO ACIDS; CELL MEMBRANES; ENZYME ACTIVITY; MAMMALS; PEPTIDES; SODIUM;

CATALYTIC MEMBRANE; CONSERVED REGIONS; FULL-LENGTH PROTEINS; NUCLEAR MAGNETIC RESONANCE(NMR); REGULATORY PROTEIN; SITE DIRECTED MUTAGENESIS; TRANS-MEMBRANE DOMAINS; TRANSMEMBRANE SEGMENTS;

ION EXCHANGE;

HYBRID PROTEIN; MALTOSE BINDING PROTEIN; MEMBRANE PROTEIN; SODIUM PROTON EXCHANGE PROTEIN 1; TRANSMEMBRANE SEGMENT 6; TRANSMEMBRANE SEGMENT 7; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; GENE MUTATION; HUMAN; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MICELLE; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; CATION TRANSPORT PROTEINS; CELLS, CULTURED; CHO CELLS; CRICETINAE; CRICETULUS; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN ISOFORMS; SODIUM-HYDROGEN ANTIPORTER;

EID: 84902177370     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500392y     Document Type: Article

References (59)

1. + exchanger: A target for cardiac therapeutic intervention Curr. Drug Targets: Cardiovasc. & Haematol. Disord. 5, 323-335
2. + exchanger in the healthy and diseased myocardium Expert Opin. Ther. Targets 13, 55-68
3. + exchanger Int. J. Mol. Med. 3, 315-321
4. + exchange and growth factor-induced cytosolic pH changes. Role in cellular proliferation Biochim. Biophys. Acta 988, 73-97
5. + Exchanger (Fliegel, L., Ed.) 101-122, R. G. Landes Co., Austin, TX.
6. Denker, S. P. and Barber, D. L. (2002) Cell migration requires both ion translocation and cytoskeletal anchoring by the Na-H exchanger NHE1 J. Cell Biol. 159, 1087-1096
7. Busco, G., Cardone, R. A., Greco, M. R., Bellizzi, A., Colella, M., Antelmi, E., Mancini, M. T., Dell'Aquila, M. E., Casavola, V., Paradiso, A., and Reshkin, S. J. (2010) NHE1 promotes invadopodial ECM proteolysis through acidification of the peri-invadopodial space FASEB J. 24, 3903-3915
8. Stock, C., Cardone, R. A., Busco, G., Krahling, H., Schwab, A., and Reshkin, S. J. (2008) Protons extruded by NHE1: Digestive or glue? Eur. J. Cell Biol. 87, 591-599
9. + antiporter in the etiopathogenesis and treatment of cancer. Two faces of the same coin - one single nature Biochim. Biophys. Acta 1756, 1-24
10. + exchanger-1 induces cytoskeletal changes involving reciprocal RhoA and Rac1 signaling, resulting in motility and invasion in MDA-MB-435 cells Breast Cancer Res. 6, R616-R628
11. + Exchanger (NHE1) in Breast Cancer Metastasis Cancer Res. 73, 1259-1264
12. + exchanger Mol. Cell. Biochem. 125, 137-143
13. Mraiche, F., Oka, T., Gan, X. T., Karmazyn, M., and Fliegel, L. (2011) Activated NHE1 is required to induce early cardiac hypertrophy in mice Basic Res. Cardiol. 106, 603-616
14. Karmazyn, M., Liu, Q., Gan, X. T., Brix, B. J., and Fliegel, L. (2003) Aldosterone increases NHE-1 expression and induces NHE-1-dependent hypertrophy in neonatal rat ventricular myocytes Hypertension 42, 1171-1176
15. + exchanger J. Mol. Cell. Cardiol. 44, 228-237
16. Murphy, E. and Allen, D. G. (2009) Why did the NHE inhibitor clinical trials fail? J. Mol. Cell. Cardiol. 46, 137-141
17. + exchanger isoform 1 J. Biol. Chem. 275, 7942-7949
18. + exchanger 1 (NHE1): Functional and clinical implications J. Biol. Chem. 282, 37854-37863
19. + exchanger isoform 1 Channels 2, 329-336
20. Cunningham, F. and Deber, C. M. (2007) Optimizing synthesis and expression of transmembrane peptides and proteins Methods 41, 370-380
21. Hunt, J. F., Earnest, T. N., Bousche, O., Kalghatgi, K., Reilly, K., Horvath, C., Rothschild, K. J., and Engelman, D. M. (1997) A biophysical study of integral membrane protein folding Biochemistry 36, 15156-15176
22. Katragadda, M., Alderfer, J. L., and Yeagle, P. L. (2001) Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin Biophys. J. 81, 1029-1036
23. + exchanger J. Biol. Chem. 285, 36656-36665
24. + exchanger Biochim. Biophys. Acta 1808, 2327-2335
25. + exchanger Can. J. Physiol. Pharmacol. 85, 319-325
26. + exchanger isoform 1 J. Biol. Chem. 281, 29817-29829
27. 2+-ATPase regulatory proteins for high-resolution structural studies Protein Expression Purif. 40, 118-125
28. + exchanger J. Biol. Chem. 280, 17863-17872
29. Schagger, H. (2006) Tricine-SDS-PAGE Nat. Protoc. 1, 16-22
30. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
31. Johnson, B. A. and Blevins, R. A. (1994) NMRView: A computer program for the visualization and analysis of NMR data J. Biomol. NMR 4, 603-614
32. Wuthrich, K. (1986) NMR of proteins and nucleic acids, Wiley, New York.
33. Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy Biochemistry 31, 1647-1651
34. Rainey, J. K., Fliegel, L., and Sykes, B. D. (2006) Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides Biochem. Cell Biol. 84, 918-929
35. Schwieters, C. D., Kuszewski, J. J., Tjandra, N., and Clore, G. M. (2003) The Xplor-NIH NMR molecular structure determination package J. Magn. Reson. 160, 65-73
36. + exchanger isoform 1 Biochem. J. 379, 31-38
37. + exchanger-directed protein kinases in the ischemic and ischemic-reperfused rat myocardium J. Biol. Chem. 27, 16113-16122
38. + antiporter potentiates growth and retinoic-acid induced differentiation of P19 embryonal carcinoma cells J. Biol. Chem. 272, 26545-26549
39. Schushan, M., Landau, M., Padan, E., and Ben-Tal, N. (2011) Two Conflicting NHE1 Model Structures: Compatibility with Experimental Data and Implications for the Transport Mechanism J. Biol. Chem. 286, le9
40. Ullah, A., Kemp, G., Lee, B., Alves, C., Young, H., Sykes, B. D., and Fliegel, L. (2013) Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2 J. Biol. Chem. 288, 24609-24624
41. + exchanger isoform 1 Biochim. Biophys. Acta 1798, 94-104
42. Hutchinson, E. G. and Thornton, J. M. (1996) PROMOTIF: A program to identify and analyze structural motifs in proteins Protein Sci. 5, 212-220
43. + exchanger J. Biol. Chem. 284, 11546-11556
44. + exchanger J. Biol. Chem. 283, 22018-22030
45. + exchanger J. Mol. Cell. Cardiol. 61, 60-67
46. + exchanger isoform 1 (NHE1) using the divide and conquer approach Biochem. Cell Biol. 89, 189-199
47. Rimon, A., Kozachkov-Magrisso, L., and Padan, E. (2012) The unwound portion dividing helix IV of NhaA undergoes a conformational change at physiological pH and lines the cation passage Biochemistry 51, 9560-9569
48. + antiporting Science 317, 799-803
49. + antiporter NhaP1 and functional role of transmembrane helix 1 EMBO J. 30, 439-449
50. Hu, N. J., Iwata, S., Cameron, A. D., and Drew, D. (2011) Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT Nature 478, 408-411
51. Lee, C., Kang, H. J., von Ballmoos, C., Newstead, S., Uzdavinys, P., Dotson, D. L., Iwata, S., Beckstein, O., Cameron, A. D., and Drew, D. (2013) A two-domain elevator mechanism for sodium/proton antiport Nature 501, 573-577
52. Salussolia, C. L., Corrales, A., Talukder, I., Kazi, R., Akgul, G., Bowen, M., and Wollmuth, L. P. (2011) Interaction of the M4 Segment with Other Transmembrane Segments Is Required for Surface Expression of Mammalian α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors J. Biol. Chem. 286, 40205-40218
53. Santiago, J., Guzman, G. R., Torruellas, K., Rojas, L. V., and Lasalde-Dominicci, J. A. (2004) Tryptophan scanning mutagenesis in the TM3 domain of the Torpedo californica acetylcholine receptor β subunit reveals an α-helical structure Biochemistry 43, 10064-10070
54. Otero-Cruz, J. D., Baez-Pagan, C. A., Caraballo-Gonzalez, I. M., and Lasalde-Dominicci, J. A. (2007) Tryptophan-scanning mutagenesis in the αM3 transmembrane domain of the muscle-type acetylcholine receptor. A spring model revealed J. Biol. Chem. 282, 9162-9171
55. + channel: Tryptophan scanning and complementation analysis lead to mutants with altered gating Biochemistry 41, 13653-13662
56. + antiporter and insights into mechanism of action and regulation by pH Nature 435, 1197-1202
57. + exchanger from Escherichia coli, in the pH-activated and ion-translocating states J. Mol. Biol. 388, 659-672
58. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8, 477-486
59. Guntert, P. (2004) Automated NMR structure calculation with CYANA Methods Mol. Biol. 278, 353-378