Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation

Plant Cell

Volumn 10, Issue 3, 1998, Pages 451-459

  Johansson, Ingela ^a   Karlsson, Maria ^a   Shukla, Vipula K ^b   Chrispeels, Maarten J ^b   Larsson, Christer ^a   Kjellbom, Per ^a  

^a LUND UNIVERSITY   (Sweden)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; SPINACIA OLERACEA; XENOPUS;

EID: 0032029335     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.10.3.451     Document Type: Article

References (40)

1. Altschul, S.F., Gish, W., Miller, W., Myers, E.W., and Lipman, D.U. (1990). Basic local alignment search tool. J. Mol. Biol. 215, 403-410.
2. Bachmann, M., Shiraishi, N., Campell, W.H., Yoo, B.-C., Harmon, A.C., and Huber, S.C. (1996). Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. Plant Cell 8, 505-517.
3. Bearden, J.C., Jr. (1978). Quantitation of submicrogram quantities of protein by an improved protein-dye binding assay. Biochim. Biophys. Acta 533, 525-529.
4. Bray, E.A. (1997). Plant responses to water deficit. Trends Plant Sci. 2, 48-54.
5. Chrispeels, M.J., and Maurel, C. (1994). Aquaporins: The molecular basis of facilitated water movement through living plant cells. Plant Physiol. 105, 9-13.
6. Cohen, P. (1989). The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58, 453-508.
7. Daniels, M.J., Mirkov, T.E., and Chrispeels, M.J. (1994). The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive aquaporin that is a homolog of the tonoplast water channel protein TIP. Plant Physiol. 106, 1325-1333.
8. Daniels, M.J., Chaumont, F., Mirkov, T.E., and Chrispeels, M.J. (1996). Characterization of a new vacuolar membrane aquaporin sensitive to mercury at a unique site. Plant Cell 8, 587-599.
9. Fray, R.G., Wallace, A., Grierson, D., and Lycett, G.W. (1994). Nucleotide sequence and expression of a ripening and water stress-related cDNA from tomato with homology to the MIP class of membrane channel proteins. Plant Mol. Biol. 24, 539-543.
10. Fushimi, K., Sasaki, S., and Marumo, F. (1997). Phosphorylation of serine 256 is required for cAMP-dependent regulatory exocytosis of the aquaporin-2 water channel. J. Biol. Chem. 272, 14800-14804.
11. Garrill, A., Findlay, G.P., and Tyerman, S.D. (1996). Mechanosensitive ion channels. In Membranes: Specialized Functions in Plants, M. Smallwood, J.P. Knox, and D.J. Bowles, eds (Oxford, UK: BIOS Scientific Publishers), pp. 247-260.
12. Guerrero, F.D., Jones, J.T., and Mullet, J.E. (1990). Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted: Sequence and expression of three inducible genes. Plant Mol. Biol. 15, 11-26.
13. Harmon, A.C., Putnam-Evans, C., and Cormier, M.J. (1987). A calcium-dependent but calmodulin-independent protein kinase from soybean. Plant Physiol. 83, 830-837.
14. Harper, J.F., Sussman, M.R., Schaller, G.E., Putman-Evans, C., Charbonneau, H., and Harmon, A.C. (1991). A calcium-dependent protein kinase with a regulatory domain similar to calmodulin. Science 252, 951-954.
15. Higuchi, R. (1990). Recombinant PCR. In PCR Protocols - A Guide to Methods and Applications, M.A. Innis, D.H. Gelfand, J.J. Sninsky, and T.J. White, eds (San Diego, CA: Academic Press), pp. 177-183.
16. 2+ and apoplastic water potential. Plant Cell 8, 1181-1191.
17. Johnson, K.D., and Chrispeels, M.J. (1992). Tonoplast-bound protein kinase phosphorylates tonoplast intrinsic protein. Plant Physiol. 100, 1787-1795.
18. Kaldenhoff, R., Kölling, A., Meyers, J., Karmann, U., Ruppel, G., and Richter, G. (1995). The blue light-responsive AthH2 gene of Arabidopsis thaliana is primarily expressed in expanding as well as in differentiating cells and encodes a putative channel protein of the ptasmalemma. Plant J. 7, 87-95.
19. Kammerloher, W., Fischer, U., Piechottka, G.P., and Schäffner, A.R. (1994). Water channels in the plant plasma membrane cloned by immunoselection from a mammalian expression system. Plant J. 6, 187-199.
20. Kase, H., Iwahashi, K., Nakanishi, S., Matsuda, Y., Yamada, K., Takahashi, M., Murakata, C., Sato, A., and Kaneko, M. (1987). K-252 compounds, novel and potent inhibitors of protein kinase C and cyclic nucleotide-dependent protein kinases. Biochem. Biophys. Res. Commun, 142, 436-440.
21. Kennelly, P.J., and Krebs, E.G. (1991). Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J. Biol. Chem. 266, 15555-15558.
22. Kuwahara, M., Fushimi, K., Terada, Y., Bai, L., Marumo, F., and Sasaki, S. (1995). cAMP-dependent phosphorylation stimulates water permeability of aquaporin-collecting duct water channel protein expressed in Xenopus oocytes. J. Biol. Chem. 270, 10384-10387.
23. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
24. Lande, M.B., Jo, I., Zeidel, M.L., Somers, M., and Harris, H.W., Jr. (1996). Phosphorylation of aquaporin-2 does not alter the membrane water permeability of rat papillary water channel-containing vesicles. J. Biol. Chem. 271, 5552-5557.
25. Larsson, C., Sommarin, M., and Widell, S. (1994). Isolation of highly purified plant plasma membranes and separation of inside-out and right-side-out vesicles. Methods Enzymol. 228, 451-469.
26. Maurel, C. (1997). Aquaporins and water permeability of plant membranes. Annu. Rev. Plant Physiol. Plant Mol. Biol. 48, 399-429.
27. Maurel, C., Kado, R.T., Guern, J., and Chrispeels, M.J. (1995). Phosphorylation regulates the water channel activity of the seed-specific aquaporin α-TIP. EMBO J. 14, 3028-3035.
28. Ohno, S., and Suzuki, K. (1995). Protein kinase C (vertebrates). In The Protein Kinase Facts Book, G. Hardie and S. Hanks, eds (London: Academic Press), pp. 80-88.
29. Park, J.H., and Saier, M.H., Jr. (1996). Phylogenetic characterization of the MIP family of transmembrane channel proteins. J. Membr. Biol. 153, 171-180.
30. Pinna, L.A., and Ruzzene, M. (1996). How do protein kinases recognize their substrates? Biochim. Biophys. Acta 1314, 191-225.
31. Preston, G.M., Carroll, T.P., Guggino, W.B., and Agre, P. (1992). Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256, 385-387.
32. Rivers, R.L., Dean, R.M., Chandy, G., Hall, J.E., Roberts, D.M., and Zeidel, M.L. (1997). Functional analysis of nodulin 26, an aquaporin in soybean root nodule symbiosomes. J. Biol. Chem. 272, 16256-16261.
33. Rosenfeld, J., Capdevielle, J., Guillemot, J.C., and Ferrara, P. (1992). In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Anal. Biochem. 203, 173-179.
34. Sharp, R.E., Silk, W.K., and Hsiao, T.C. (1988). Growth of the maize primary root at low water potentials. I. Spatial distribution of expansive growth. Plant Physiol. 87, 50-57.
35. Tischler, A.S., Ruzicka, L.A., and Perlman, R.L. (1990). Mimicry and inhibition of nerve growth factor effects: Interactions of staurosporin, forskolin and K252a in PC12 cells and normal rat chromaffin cells in vitro. J. Neurochem. 55, 1159-1165.
36. Weaver, C.D., and Roberts, D.M. (1992). Determination of the site of phosphorylation of nodulin 26 by the calcium-dependent protein kinase from soybean nodules. Biochemistry 31, 8954-8959.
37. Weaver, C.D., Crombie, B., Stacey, G., and Roberts, D.M. (1991). Calcium-dependent phosphorylation of symbiosome membrane proteins from nitrogen-fixing soybean nodules. Plant Physiol. 95, 222-227.
38. Weig, A., Deswartes, C., and Chrispeels, M.J. (1997). The major intrinsic protein family of Arabidopsis has 23 members that form three distinct groups with functional aquaporins in each group. Plant Physiol. 114, 1347-1357.
39. Yamaguchi-Shinozaki, K., Koizumi, M., Urao, S., and Shinozaki, K. (1992). Molecular cloning and characterization of 9 cDNAs for genes that are responsive to desiccation in Arabidopsis thaliana: Sequence analysis of one cDNA clone that encodes a putative transmembrane channel protein. Plant Cell Physiol. 33, 217-224.
40. Zhang, R., and Verkman, A.S. (1991). Water and urea permeability properties of Xenopus oocytes: Expression of mRNA from toad urinary bladder. Am. J. Physiol. 260, C26-C34.