메뉴 건너뛰기




Volumn 289, Issue 42, 2014, Pages 29273-29284

Short forms of Ste20-related proline/alanine-rich kinase (SPAK) in the kidney are created by aspartyl aminopeptidase (Dnpep)-mediated proteolytic cleavage

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD PRESSURE;

EID: 84908093597     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.604009     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 78751654853 scopus 로고    scopus 로고
    • The WNKs: Atypical protein kinases with pleiotropic actions
    • McCormick, J. A., and Ellison, D. H. (2011) The WNKs: Atypical protein kinases with pleiotropic actions. Physiol. Rev. 91, 177-219.
    • (2011) Physiol. Rev. , vol.91 , pp. 177-219
    • McCormick, J.A.1    Ellison, D.H.2
  • 2
    • 84867733611 scopus 로고    scopus 로고
    • Molecular physiology of SPAK and OSR1: Two Ste20-related protein kinases regulating ion transport
    • Gagnon, K. B., and Delpire, E. (2012) Molecular physiology of SPAK and OSR1: Two Ste20-related protein kinases regulating ion transport. Physiol. Rev. 92, 1577-1617.
    • (2012) Physiol. Rev. , vol.92 , pp. 1577-1617
    • Gagnon, K.B.1    Delpire, E.2
  • 3
    • 38749087627 scopus 로고    scopus 로고
    • SPAK and OSR1: STE20 kinases involved in the regulation of ion homoeostasis and volume control in mammalian cells
    • Delpire, E., and Gagnon, K. B. (2008) SPAK and OSR1: STE20 kinases involved in the regulation of ion homoeostasis and volume control in mammalian cells. Biochem. J. 409, 321-331.
    • (2008) Biochem. J. , vol.409 , pp. 321-331
    • Delpire, E.1    Gagnon, K.B.2
  • 4
    • 30644458584 scopus 로고    scopus 로고
    • Volume sensitivity of cation chloride cotransporters is modulated by the interaction of two kinases: SPAK and WNK4
    • Gagnon, K. B., England, R., and Delpire, E. (2006) Volume sensitivity of cation chloride cotransporters is modulated by the interaction of two kinases: SPAK and WNK4. Am. J. Physiol. Cell Physiol. 290, C134-C142.
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290 , pp. C134-C142
    • Gagnon, K.B.1    England, R.2    Delpire, E.3
  • 5
    • 30644472724 scopus 로고    scopus 로고
    • Characterization of SPAK and OSR1, regulatory kinases of the Na-K-2Cl cotransporter
    • Gagnon, K. B., England, R., and Delpire, E. (2006) Characterization of SPAK and OSR1, regulatory kinases of the Na-K-2Cl cotransporter. Mol. Cell. Biol. 26, 689-698.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 689-698
    • Gagnon, K.B.1    England, R.2    Delpire, E.3
  • 6
    • 83755225807 scopus 로고    scopus 로고
    • Functional insights into the activation mechanism of Ste20-related kinases
    • Gagnon, K. B., Rios, K., and Delpire, E. (2011) Functional insights into the activation mechanism of Ste20-related kinases. Cell. Physiol. Biochem. 28, 1219-1230.
    • (2011) Cell. Physiol. Biochem. , vol.28 , pp. 1219-1230
    • Gagnon, K.B.1    Rios, K.2    Delpire, E.3
  • 10
    • 0037184942 scopus 로고    scopus 로고
    • Cation-chloride cotransporters interact with the stress-related kinases SPAK and OSR1
    • Piechotta, K., Lu, J., and Delpire, E. (2002) Cation-chloride cotransporters interact with the stress-related kinases SPAK and OSR1. J. Biol. Chem. 277, 50812-50819.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50812-50819
    • Piechotta, K.1    Lu, J.2    Delpire, E.3
  • 11
    • 35548971082 scopus 로고    scopus 로고
    • Structural insights into the recognition of substrates and activators by the OSR1 kinase
    • Villa, F., Goebel, J., Rafiqi, F. H., Deak, M., Thastrup, J., Alessi, D. R., and van Aalten, D. M. (2007) Structural insights into the recognition of substrates and activators by the OSR1 kinase. EMBO Rep. 8, 839-845.
    • (2007) EMBO Rep , vol.8 , pp. 839-845
    • Villa, F.1    Goebel, J.2    Rafiqi, F.H.3    Deak, M.4    Thastrup, J.5    Alessi, D.R.6    Van Aalten, D.M.7
  • 12
    • 67649771374 scopus 로고    scopus 로고
    • The Ste20 kinases SPAK and OSR1 regulate NKCC1 function in sensory neurons
    • Geng, Y., Hoke, A., and Delpire, E. (2009) The Ste20 kinases SPAK and OSR1 regulate NKCC1 function in sensory neurons. J. Biol. Chem. 284, 14020-14028.
    • (2009) J. Biol. Chem. , vol.284 , pp. 14020-14028
    • Geng, Y.1    Hoke, A.2    Delpire, E.3
  • 18
    • 84890365274 scopus 로고    scopus 로고
    • Regulation of NKCC2 activity by inhibitory SPAK isoforms: KS-SPAK is a more potent inhibitor than SPAK2
    • Park, H. J., Curry, J. N., and McCormick, J. A. (2013) Regulation of NKCC2 activity by inhibitory SPAK isoforms: KS-SPAK is a more potent inhibitor than SPAK2. Am. J. Physiol. Renal Physiol. 305, F1687-F1696.
    • (2013) Am. J. Physiol. Renal Physiol. , vol.305 , pp. F1687-F1696
    • Park, H.J.1    Curry, J.N.2    McCormick, J.A.3
  • 19
    • 0346101747 scopus 로고    scopus 로고
    • - cotransporter in the nervous system: Evidence for a scaffolding role of the kinase
    • - cotransporter in the nervous system: evidence for a scaffolding role of the kinase. J. Biol. Chem. 278, 52848-52856.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52848-52856
    • Piechotta, K.1    Garbarini, N.2    England, R.3    Delpire, E.4
  • 22
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J. R., Eng, J. K., McCormack, A. L., and Schieltz, D. (1995) Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem. 67, 1426-1436.
    • (1995) Anal. Chem. , vol.67 , pp. 1426-1436
    • Yates, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 24
    • 0347445722 scopus 로고    scopus 로고
    • A genomic analysis of rat proteases and protease inhibitors
    • Puente, X. S., and López-Otín, C. (2004) A genomic analysis of rat proteases and protease inhibitors. Genome Res. 14, 609-622.
    • (2004) Genome Res , vol.14 , pp. 609-622
    • Puente, X.S.1    López-Otín, C.2
  • 25
    • 33947482089 scopus 로고
    • Dithiothreitol. A new protective reagent for SH groups
    • Cleland, W. W. (1964) Dithiothreitol. A new protective reagent for SH groups. Biochemistry 3, 480-482.
    • (1964) Biochemistry , vol.3 , pp. 480-482
    • Cleland, W.W.1
  • 28
    • 0032569016 scopus 로고    scopus 로고
    • Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase
    • Wilk, S., Wilk, E., and Magnusson, R. P. (1998) Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase. J. Biol. Chem. 273, 15961-15970.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15961-15970
    • Wilk, S.1    Wilk, E.2    Magnusson, R.P.3
  • 29
    • 33644878272 scopus 로고    scopus 로고
    • Identification of yeast aspartyl aminopeptidase gene by purifying and characterizing its product from yeast cells
    • Yokoyama, R., Kawasaki, H., and Hirano, H. (2006) Identification of yeast aspartyl aminopeptidase gene by purifying and characterizing its product from yeast cells. FEBS J. 273, 192-198.
    • (2006) FEBS J , vol.273 , pp. 192-198
    • Yokoyama, R.1    Kawasaki, H.2    Hirano, H.3
  • 30
    • 84859771335 scopus 로고    scopus 로고
    • Insights into substrate specificity and metal activation of mammalian tetrahedral aspartyl aminopeptidase
    • Chen, Y., Farquhar, E. R., Chance, M. R., Palczewski, K., and Kiser, P. D. (2012) Insights into substrate specificity and metal activation of mammalian tetrahedral aspartyl aminopeptidase. J. Biol. Chem. 287, 13356-13370.
    • (2012) J. Biol. Chem. , vol.287 , pp. 13356-13370
    • Chen, Y.1    Farquhar, E.R.2    Chance, M.R.3    Palczewski, K.4    Kiser, P.D.5
  • 31
    • 84862491849 scopus 로고    scopus 로고
    • Structure of human aspartyl aminopeptidase complexed with substrate analogue: Insight into catalytic mechanism, substrate specificity and M18 peptidase family
    • Chaikuad, A., Pilka, E. S., De Riso, A., von Delft, F., Kavanagh, K. L., Vénien-Bryan, C., Oppermann, U., and Yue, W. W. (2012) Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family. BMC Struct. Biol. 12, 14.
    • (2012) BMC Struct. Biol. , vol.12 , pp. 14
    • Chaikuad, A.1    Pilka, E.S.2    De Riso, A.3    Von Delft, F.4    Kavanagh, K.L.5    Vénien-Bryan, C.6    Oppermann, U.7    Yue, W.W.8
  • 32
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the Phyre server
    • Kelley, L. A., and Sternberg, M. J. (2009) Protein structure prediction on the web: A case study using the Phyre server. Nat. Protoc. 4, 363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 33
    • 35848939568 scopus 로고    scopus 로고
    • Human and mouse homo-oligomeric meprin A metalloendopeptidase: Substrate and inhibitor specificities
    • Bylander, J. E., Bertenshaw, G. P., Matters, G. L., Hubbard, S. J., and Bond, J. S. (2007) Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities. Biol. Chem. 388, 1163-1172.
    • (2007) Biol. Chem. , vol.388 , pp. 1163-1172
    • Bylander, J.E.1    Bertenshaw, G.P.2    Matters, G.L.3    Hubbard, S.J.4    Bond, J.S.5
  • 34
    • 0034661399 scopus 로고    scopus 로고
    • Noncompetitive, reversible inhibition of aminoacylase-1 by a series of L-α-hydroxyl and L-α-fluoro fatty acids: Ligand specificity of aspergillus oryzae and porcine kidney enzymes
    • Tamura, T., Oki, Y., Yoshida, A., Kuriyama, T., Kawakami, H., Inoue, H., Inagaki, K., and Tanaka, H. (2000) Noncompetitive, reversible inhibition of aminoacylase-1 by a series of L-α-hydroxyl and L-α-fluoro fatty acids: ligand specificity of aspergillus oryzae and porcine kidney enzymes. Arch. Biochem. Biophys. 379, 261-266.
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 261-266
    • Tamura, T.1    Oki, Y.2    Yoshida, A.3    Kuriyama, T.4    Kawakami, H.5    Inoue, H.6    Inagaki, K.7    Tanaka, H.8
  • 38
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson, M. P. (1994) The structure and function of proline-rich regions in proteins. Biochem. J. 297, 249-260.
    • (1994) Biochem. J. , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 39
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay, B. K., Williamson, M. P., and Sudol, M. (2000) The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231-241.
    • (2000) FASEB J , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 40
    • 0016156286 scopus 로고
    • The amino-acid sequence of the alkali light chains of rabbit skeletal-muscle myosin
    • Frank, G., and Weeds, A. G. (1974) The amino-acid sequence of the alkali light chains of rabbit skeletal-muscle myosin. Eur. J. Biochem. 44, 317-334.
    • (1974) Eur. J. Biochem. , vol.44 , pp. 317-334
    • Frank, G.1    Weeds, A.G.2
  • 42
    • 0034011237 scopus 로고    scopus 로고
    • Integrative aspects of zinc transporters
    • Cousins, R. J., and McMahon, R. J. (2000) Integrative aspects of zinc transporters. J. Nutr. 130, 1384S-1387S.
    • (2000) J. Nutr. , vol.130 , pp. 1384S-1387S
    • Cousins, R.J.1    McMahon, R.J.2
  • 43
    • 0036890215 scopus 로고    scopus 로고
    • Intracellular distribution of labile Zn(II) and zinc transporter expression in kidney and MDCK cells
    • Ranaldi, G., Perozzi, G., Truong-Tran, A., Zalewski, P., and Murgia, C. (2002) Intracellular distribution of labile Zn(II) and zinc transporter expression in kidney and MDCK cells. Am. J. Physiol. Renal Physiol. 283, F1365-F1375.
    • (2002) Am. J. Physiol. Renal Physiol. , vol.283 , pp. F1365-F1375
    • Ranaldi, G.1    Perozzi, G.2    Truong-Tran, A.3    Zalewski, P.4    Murgia, C.5
  • 44
    • 0030692035 scopus 로고    scopus 로고
    • Aminopeptidase A: A key enzyme in the intrarenal degradation of angiotensin II
    • Wolf, G., Mentzel, S., and Assmann, K. J. (1997) Aminopeptidase A: A key enzyme in the intrarenal degradation of angiotensin II. Exp. Nephrol. 5, 364-369.
    • (1997) Exp. Nephrol. , vol.5 , pp. 364-369
    • Wolf, G.1    Mentzel, S.2    Assmann, K.J.3
  • 47
    • 68949094195 scopus 로고    scopus 로고
    • ENaC at the cutting edge: Regulation of epithelial sodium channels by proteases
    • Kleyman, T. R., Carattino, M. D., and Hughey, R. P. (2009) ENaC at the cutting edge: regulation of epithelial sodium channels by proteases. J. Biol. Chem. 284, 20447-20451.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20447-20451
    • Kleyman, T.R.1    Carattino, M.D.2    Hughey, R.P.3
  • 48
    • 64149083549 scopus 로고    scopus 로고
    • Activation of the epithelial sodiumchannel (ENaC) by serine proteases
    • Rossier, B. C., and Stutts, M. J. (2009) Activation of the epithelial sodiumchannel (ENaC) by serine proteases. Annu. Rev. Physiol. 71, 361-379.
    • (2009) Annu. Rev. Physiol. , vol.71 , pp. 361-379
    • Rossier, B.C.1    Stutts, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.