Domain swapping in the kinase superfamily: OSR1 joins the mix

Protein Science

Volumn 18, Issue 4, 2009, Pages 678-681

  Li, Ying ^a   Palmer III, Arthur G ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE; COTRANSPORTER; CYCLIN DEPENDENT KINASE 2; DIMER; MITOGEN ACTIVATED PROTEIN KINASE; MONOMER; OLIGOMER; OXIDATIVE STRESS RESPONSIVE 1 PROTEIN; P21 ACTIVATED KINASE 1; POTASSIUM ION; PROTEIN KINASE; PROTEIN KINASE WNK1; PROTEIN KINASE WNK4; REGULATOR PROTEIN; SODIUM ION; UNCLASSIFIED DRUG;

AUTOPHOSPHORYLATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DIMERIZATION; DOMAIN SWAPPING; ENZYME ACTIVE SITE; ENZYME CONFORMATION; HUMAN; NOTE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN INTERACTION; SIGNAL TRANSDUCTION; STRUCTURAL HOMOLOGY;

EID: 63449106913     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.98     Document Type: Note

References (26)

1. Manning 6, Whyte DB, Martinez R. Hunter T, Sudarsa-nam S (2002) The protein kinase complement of the human genome. Science 298:1912-1934.
2. Goldsmith EJ, Akella R, Min X, Zhou T, Humphreys JM (2007) Substrate and docking interactions in serine/threonine protein kinases. Chem Rev 107:5065-5081.
3. Oliver AW, Paul A, Boxall KJ, Barrie SE, Aherne GW, Garrett MD, Mittnacht S, Pearl LH (2006) Trans activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange. EMBO J 25:3179-3190.
4. Pike AC, Relics P, Niesen FH, Tumbull A, Oliver AW, Parker SA, Turk BE, Pearl LH, Knapp S (2008) Activation segment dimerization: a mechanism for kinase autophos-phorylation of non-consensus sites. EMBO J 27:704-714.
5. Lee S-J, Cobb MH, Goldsmith EJ (2009) Crystal structure of domain-swapped ste20 OSRi kinase domain. Protein Sci 18:304-313.
6. Villa F, Deak M, Alessi DR, van Aalten DM (2008) Structure of the OSR1 kinase, a hypertension drug target. Proteins 73:1082-1087.
7. Chen W, Yazicioglu M, Cobb MH (2004) Characterization of OSR1, a member of the mammalian Ste2op/germinal center kinase subfamily. J Biol Chem 279:11129-11136.
8. Kahle KT, Rinehart J, Ring A, Gimenez I, Gamba G, Hebert SC, Lifton RP (2006) WNK protein kinases modulate cellular CI- flux by altering the phosphorylation state of the Na-K-Cl and K-Cl cotransporters. Physiology 21:326-335.
9. Vitari AC, Deak M, Morrice NA, Alessi DR (2005) The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases. Biochem J 391:17-24.
10. Anselmo AN, Earnest S, Chen W, Juang YC, Kim SC, Zhao Y, Cobb MH (2006) WNK1 and OSR1 regulate the Na+, K+, 2CI- cotransporter in HeLa cells. Proc Natl Acad Sci USA 103:10883-10888.
11. Wilson FH, Disse-Nicodeme S, Choate KA, Ishikawa K, Nelson-Williams C, Desitter I, Gunel M, Milford DV, Lip- kin GW, Achard JM, Feely MP, Dussol B, Berland Y, Unwin RJ, Mayan H, Simon DB, Farfel Z, Jeunemaitre X, Lifton RP (2001) Human hypertension caused by mutations in WNK kinases. Science 293:1107-1112.
12. Johnson LN, Noble ME, Owen DJ (1996) Active and inactive protein kinases: structural basis for regulation. Cell 85:149-158.
13. Song H, Hanlon N, Brown NR. Noble ME, Johnson LN, Bar- ford D (2001) Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. Mol Cell 7:615-626.
14. Pirruccello M, Sondermann H, Pelton JG, Pellicena P, Hoelz A, Chernoff J, Wemmer DE, Kuriyan J (2006) A dimeric kinase assembly underlying autophosphorylation in the p21 activated kinases. J Mol Biol 361:312-326.
15. Lei M, Robinson MA. Harrison SC (2005) The active conformation of the PAK1 kinase domain. Structure 13:769-778.
16. De Bondt HL, Rosenblatt J, Jancarik J, Jones HD, Morgan DO, Kim SH (1993) Crystal structure of cyclin-de-pendent kinase 2. Nature 363:595-602.
17. Min X, Lee BH, Cobb MH, Goldsmith EJ (2004) Crystal structure of the kinase domain of WNK1, a kinase that causes a hereditary form of hypertension. Structure 12:1303-1311
18. Ohren JF, Chen H. Pavlovsky A, Whitehead C, Zhang E, Kuffa P, Yan C, McDonnell P, Spessard C, Banotai C, Mueller WT, Delaney A, Omer C, Sebolt-Leopold J, Dudley DT, Leung IK, Flamme C, Warmus J, Kaufman M, Barrett S, Tecle H, Hasemann CA (2004) Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition. Nat Struct Mol Biol 11:1192-1197.
19. Liu Y, Eisenberg D (2002) 3D domain swapping: as domains continue to swap. Protein Sci 11:1285-1299.
20. Carey J, Lindman S, Bauer M, Linse S (2007) Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency. Protein Sci 16: 2317-2333.
21. Huse M, Kuriyan J (2002) The conformational plasticity of protein kinases. Cell 109:275-282.
22. Li F, Gangal M, Juliano C, Gorfain E, Taylor SS, Johnson DA (2002) Evidence for an internal entropy contribution to phosphoryi transfer: a study of domain closure, backbone flexibility, and the catalytic cycle of cAMP-depend-ent protein kinase. J Mol Biol 315:459-469.
23. Vajpai N, Strauss A, Fendrich G, Cowan-Jacob SW, Man-ley PW, Grzesiek S, Janke W (2008) Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib. J Biol Chem 283:18292-18302.
24. Vogtherr M, Saxena K, Hoelder S, Grimme S, Betz M, Schieborr U, Pescatore B, Robin M, Delarbre L, Langer T, Wendt KU, Schwalbe H (2006) NMR characterization of kinase p38 dynamics in free and ligand-bound forms. Angew Chem Int Ed Engl 45:993-997.
25. Miloushev VZ, Bahna F, Ciatto C, Ahlsen G, Honig B, Shapiro L, Palmer AG (2008) Dynamic properties of a type II cadherin adhesive domain: implications for the mechanism of strand-swapping of classical cadherins. Structure 16:1195-1205.
26. Seeliger MA. Spichty M, Kelly SE, Bycroft M, Freund SM, Karplus M, Itzhaki LS (2005) Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins. J Biol Chem 280:30448-30459.