The Sam domain of the lipid phosphatase ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam

BMC Structural Biology

Volumn 9, Issue , 2009, Pages

  Leone, Marilisa ^a   Cellitti, Jason ^a   Pellecchia, Maurizio ^a  

^a BURNHAM INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPHRIN A2; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PROTEIN ARAP3; PROTEIN TYROSINE PHOSPHATASE SHP 2; UNCLASSIFIED DRUG; ARAP3 PROTEIN, HUMAN; EPHRIN RECEPTOR A2; INPPL1 PROTEIN, HUMAN; PHOSPHATASE; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

ARTICLE; DIMERIZATION; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR MODEL; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; STERILE ALPHA MOTIF DOMAIN; AMINO ACID SEQUENCE; CHEMISTRY; COMPUTER SIMULATION; HUMAN; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; COMPUTER SIMULATION; GTPASE-ACTIVATING PROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; RECEPTOR, EPHA2; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 70350755888     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-9-59     Document Type: Article

References (36)

1. ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner. ST I Z Nie A Stewart M Najdovska NE Hall H He PA Randazzo P Lock, J Cell Sci 2004 117 Pt 25 6071 6084 15546919
2. Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices. S Krugmann KE Anderson SH Ridley N Risso A McGregor J Coadwell K Davidson A Eguinoa CD Ellson P Lipp, et al. Mol Cell 2002 9 1 95 108 10.1016/S1097-2765(02) 00434-3 11804589
3. The PI3K effector Arap3 interacts with the PI(3,4,5)P(3) phosphatase SHIP2 in a SAM domain-dependent manner. JH Raaijmakers L Deneubourg H Rehmann J de Koning Z Zhang S Krugmann C Erneux JL Bos, Cell Signal 2007 19 6 1249 1257 10.1016/j.cellsig.2006.12.015 17314030
4. ARAP3 is a PI3K- and rap-regulated GAP for RhoA. S Krugmann R Williams L Stephens PT Hawkins, Curr Biol 2004 14 15 1380 1384 10.1016/j.cub.2004.07.058 15296756
5. Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. X Pesesse S Deleu F De Smedt L Drayer C Erneux, Biochem Biophys Res Commun 1997 239 3 697 700 10.1006/bbrc.1997.7538 9367831
6. The SH2 domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity. X Pesesse C Moreau AL Drayer R Woscholski P Parker C Erneux, FEBS Lett 1998 437 3 301 303 10.1016/S0014-5793(98)01255-1 9824312
7. Regulation of enzyme localization by polymerization: polymer formation by the SAM domain of diacylglycerol kinase delta1. BT Harada MJ Knight S Imai F Qiao R Ramachander MR Sawaya M Gingery F Sakane JU Bowie, Structure 2008 16 3 380 387 10.1016/j.str.2007.12.017 18334213
8. CNK and HYP form a discrete dimer by their SAM domains to mediate RAF kinase signaling. T Rajakulendran M Sahmi I Kurinov M Tyers M Therrien F Sicheri, Proc Natl Acad Sci USA 2008 105 8 2836 2841 10.1073/pnas.0709705105 18287031
9. SAM domains can utilize similar surfaces for the formation of polymers and closed oligomers. R Ramachander JU Bowie, J Mol Biol 2004 342 5 1353 1358 10.1016/j.jmb.2004.08.011 15364564
10. NMR studies of a heterotypic Sam-Sam domain association: the interaction between the lipid phosphatase Ship2 and the EphA2 receptor. M Leone J Cellitti M Pellecchia, Biochemistry 2008 47 48 12721 12728 10.1021/bi801713f 18991394
11. Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphatidylinositol 3-Kinase-dependent Rac1 activation. G Zhuang S Hunter Y Hwang J Chen, J Biol Chem 2007 282 4 2683 2694 10.1074/jbc.M608509200 17135240
12. Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site. CM Slupsky LN Gentile LW Donaldson CD Mackereth JJ Seidel BJ Graves LP McIntosh, Proc Natl Acad Sci USA 1998 95 21 12129 12134 10.1073/pnas.95.21.12129 9770451
13. Solution structure of the receptor tyrosine kinase EphB2 SAM domain and identification of two distinct homotypic interaction sites. M Smalla P Schmieder M Kelly A Ter Laak G Krause L Ball M Wahl P Bork H Oschkinat, Protein Sci 1999 8 10 1954 1961 10.1110/ps.8.10.1954 10548040
14. Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex. S Bhattacharjya P Xu R Gingras R Shaykhutdinov C Wu M Whiteway F Ni, J Mol Biol 2004 344 4 1071 1087 10.1016/j.jmb.2004.09.018 15544813
15. NMR in drug discovery. M Pellecchia DS Sem K Wuthrich, Nat Rev Drug Discov 2002 1 3 211 219 10.1038/nrd748 12120505
16. Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions. M Pellecchia, Chem Biol 2005 12 9 961 971 10.1016/j.chembiol.2005.08.013 16183020
17. Localizing the NADP+ binding site on the MurB enzyme by NMR. BT Farmer 2nd KL Constantine V Goldfarb MS Friedrichs M Wittekind J Yanchunas Jr JG Robertson L Mueller, Nat Struct Biol 1996 3 12 995 997 10.1038/nsb1296-995 8946851
18. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. C Dominguez R Boelens AM Bonvin, J Am Chem Soc 2003 125 7 1731 1737 10.1021/ja026939x 12580598
19. Monitoring the effects of antagonists on protein-protein interactions with NMR spectroscopy. L D'Silva P Ozdowy M Krajewski U Rothweiler M Singh TA Holak, J Am Chem Soc 2005 127 38 13220 13226 10.1021/ja052143x 16173750
20. The many faces of SAM. F Qiao JU Bowie, Sci STKE 2005 2005 286 e7 10.1126/stke.2862005re7 15928333
21. SAM domains: uniform structure, diversity of function. CA Kim JU Bowie, Trends Biochem Sci 2003 28 12 625 628 10.1016/j.tibs.2003.11.001 14659692
22. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. SF Altschul TL Madden AA Schaffer J Zhang Z Zhang W Miller DJ Lipman, Nucleic Acids Res 1997 25 17 3389 3402 10.1093/nar/25.17.3389 9254694
23. Announcing the worldwide Protein Data Bank. H Berman K Henrick H Nakamura, Nat Struct Biol 2003 10 12 980 10.1038/nsb1203-980 14634627 (Pubitemid 37500485)
24. The SAM domain of polyhomeotic forms a helical polymer. CA Kim M Gingery RM Pilpa JU Bowie, Nat Struct Biol 2002 9 6 453 457 11992127
25. Derepression by depolymerization; structural insights into the regulation of Yan by Mae. F Qiao H Song CA Kim MR Sawaya JB Hunter M Gingery I Rebay AJ Courey JU Bowie, Cell 2004 118 2 163 173 10.1016/j.cell.2004.07.010 15260987
26. Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression. CA Kim ML Phillips W Kim M Gingery HH Tran MA Robinson S Faham JU Bowie, EMBO J 2001 20 15 4173 4182 10.1093/emboj/20.15.4173 11483520
27. Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling. D Neri T Szyperski G Otting H Senn K Wuthrich, Biochemistry 1989 28 19 7510 7516 10.1021/bi00445a003 2692701
28. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. C Bartels TH Xia M Billeter P Güntert K Wüthrich, J Biomol NMR 1995 5 1 10 10.1007/BF00417486 7881269
29. Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. S Grzesiek A Bax, J Biomol NMR 1993 3 2 185 204 10.1007/BF00178261 8477186
30. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. T Herrmann P Guntert K Wuthrich, J Mol Biol 2002 319 1 209 227 10.1016/S0022-2836(02)00241-3 12051947
31. An optimized 3D NOESY-HSQC. S Talluri G Wagner, J Magn Reson B 1996 112 2 200 205 10.1006/jmrb.1996.0132 8812906
32. A 2D nuclear Overhauser enhancement (2D NOE) experiment for elucidation of complete proton-proton cross relaxation networks in biological macromolecules. A Kumar RR Ernst K Wuthrich, Biochm Biophys Res Commun 1980 95 1 6 10.1016/0006-291X(80)90695-6
33. MOLMOL: a program for display and analysis of macromolecular structures. R Koradi M Billeter K Wuthrich, J Mol Graph 1996 14 1 51 55 29-32. 10.1016/0263-7855(96)00009-4 8744573
34. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. RA Laskowski JA Rullmannn MW MacArthur R Kaptein JM Thornton, J Biomol NMR 1996 8 4 477 486 10.1007/BF00228148 9008363
35. Texture mapping: a new tool for molecular graphics. M Teschner C Henn H Vollhardt S Reiling J Brickmann, J Mol Graph 1994 12 2 98 105 10.1016/0263-7855(94)80074-X 7918258
36. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. JD Thompson DG Higgins TJ Gibson, Nucleic Acids Res 1994 22 22 4673 4680 10.1093/nar/22.22.4673 7984417