Water channel aquaporin-2 directly binds to actin

Biochemical and Biophysical Research Communications - Tập 322 Số 3 - Trang 740-745 - 2004
Yumi Noda1,2, Saburo Horikawa3, Yoshifumi Katayama1, Sei Sasaki2
1Department of Autonomic Physiology, Tokyo Medical and Dental University, Tokyo 113-8519, Japan
2Department of Nephrology, Tokyo Medical and Dental University, Tokyo 113-8519, Japan
3Department of Pathological Biochemistry, Tokyo Medical and Dental University, Tokyo 113-8519, Japan

Tóm tắt

Từ khóa


Tài liệu tham khảo

Nielsen, 2002, Aquaporins in the kidney: from molecules to medicine, Physiol. Rev., 82, 205, 10.1152/physrev.00024.2001

Fushimi, 1993, Cloning and expression of apical membrane water channel of rat kidney collecting tubule, Nature, 361, 549, 10.1038/361549a0

Kamsteeg, 2000, The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers, J. Cell Biol., 151, 919, 10.1083/jcb.151.4.919

Yang, 2001, Neonatal mortality in an aquaporin-2 knock-in mouse model of recessive nephrogenic diabetes insipidus, J. Biol. Chem., 276, 2775, 10.1074/jbc.M008216200

Kamsteeg, 1999, An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus, EMBO J., 18, 2394, 10.1093/emboj/18.9.2394

Kuwahara, 2001, Three families with autosomal dominant nephrogenic diabetes insipidus caused by aquaporin-2 mutations in the C-terminus, Am. J. Hum. Genet., 69, 738, 10.1086/323643

Marr, 2002, Heteroligomerization of an aquaporin-2 mutant with wild-type aquaporin-2 and their misrouting to late endosomes/lysosomes explains dominant nephrogenic diabetes insipidus, Hum. Mol. Genet., 11, 779, 10.1093/hmg/11.7.779

Yamashita, 2000, Mutations in sixth transmembrane domain of AQP2 inhibit its translocation induced by vasopressin, Am. J. Physiol., 278, F395

O’Farrell, 1975, High resolution two-dimensional electrophoresis of proteins, J. Biol. Chem., 250, 4007, 10.1016/S0021-9258(19)41496-8

Shevchenko, 1996, Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels, Anal. Chem., 68, 850, 10.1021/ac950914h

Vandekerckhove, 1979, The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A protein-chemical analysis of muscle actin differentiation, Differentiation, 14, 123, 10.1111/j.1432-0436.1979.tb01021.x

Nunoi, 1999, A heterozygous mutation of beta-actin associated with neutrophil dysfunction and recurrent infection, Proc. Natl. Acad. Sci. USA, 96, 8693, 10.1073/pnas.96.15.8693

Szymanski, 1998, Differences in contractile protein content and isoforms in phasic and tonic smooth muscles, Am. J. Physiol., 273, C684, 10.1152/ajpcell.1998.275.3.C684

Suzuki, 1998, Decrease in gamma-actin expression, disruption of actin microfilaments and alterations in cell adhesion systems associated with acquisition of metastatic capacity in human salivary gland adenocarcinoma cell clones, Int. J. Oncol., 12, 1079

Mattila, 2003, Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its C-terminal WH2 domain, J. Biol. Chem., 10, 8452, 10.1074/jbc.M212113200

Pollard, 2000, Molecular mechanisms controlling actin filament dynamics in nonmuscle cells, Annu. Rev. Biophys. Biomol. Struct., 29, 545, 10.1146/annurev.biophys.29.1.545

Ojala, 2002, The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers, Mol. Biol. Cell, 13, 3811, 10.1091/mbc.e02-03-0157

Tamura, 2000, Direct interaction of actin with p47(phox) of neutrophil NADPH oxidase, Biochem. Biophys. Res. Commun., 276, 1186, 10.1006/bbrc.2000.3598

Van Troys, 1999, Structural modules in actin-binding proteins: towards a new classification, Biochim. Biophys. Acta, 1448, 323, 10.1016/S0167-4889(98)00152-9

Klussmann, 2001, An inhibitory role of Rho in the vasopressin-mediated translocation of aquaporin-2 into cell membranes of renal principal cells, J. Biol. Chem., 276, 20451, 10.1074/jbc.M010270200