Interactions between kinase scaffold MP1/p14 and its endosomal anchoring protein p18

Biochemistry

Volumn 50, Issue 18, 2011, Pages 3696-3705

  Magee, James ^a   Cygler, Miroslaw ^a  

^a NATIONAL RESEARCH COUNCIL CANADA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEINS; BINDING PARTNERS; CO-EXPRESSION; DENATURED STATE; DISSOCIATION CONSTANT; E. COLI; ENDOSOMAL COMPARTMENTS; ENDOSOMAL MEMBRANE; HETERODIMERS; IN-VITRO; INCLUSION BODIES; LATE ENDOSOMES; MICROMOLAR RANGE; MOLTEN GLOBULE; SCAFFOLD PROTEIN; SIGNALING CASCADES; SIGNALING COMPLEX; SOLUBLE PROTEINS; SPATIAL ORGANIZATION; TERMINAL RESIDUES;

DISSOCIATION; ESCHERICHIA COLI; PROTEINS; SIGNALING; TETHERLINES;

SCAFFOLDS (BIOLOGY);

CELL PROTEIN; ENDOSOMAL ANCHORING PROTEIN P18; PHOSPHOTRANSFERASE; PROTEIN MP1; RECOMBINANT PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; ENDOSOME; MOLECULAR CLONING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; STOICHIOMETRY;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; CALORIMETRY; CIRCULAR DICHROISM; CLONING, MOLECULAR; CYTOPLASM; DIMERIZATION; ESCHERICHIA COLI; EXTRACELLULAR SIGNAL-REGULATED MAP KINASES; GENE DELETION; MICE; MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS;

EID: 79955574252     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101972y     Document Type: Article

References (29)

1. Skarpen, E., Flinder, L. I., Rosseland, C. M., Orstavik, S., Wierod, L., Oksvold, M. P., Skalhegg, B. S., and Huitfeldt, H. S. (2008) MEK1 and MEK2 regulate distinct functions by sorting ERK2 to different intracellular compartments FASEB J. 22, 466-476 (Pubitemid 351225583)
2. Severin, S., Ghevaert, C., and Mazharian, A. (2010) The mitogen-activated protein kinase signaling pathways: role in megakaryocyte differentiation J. Thromb. Haemost. 8, 17-26
3. Mebratu, Y. and Tesfaigzi, Y. (2009) How ERK1/2 activation controls cell proliferation and cell death: Is subcellular localization the answer? Cell Cycle 8, 1168-1175
4. Montagut, C. and Settleman, J. (2009) Targeting the RAF-MEK-ERK pathway in cancer therapy Cancer Lett. 283, 125-134
5. Aoki, Y., Niihori, T., Narumi, Y., Kure, S., and Matsubara, Y. (2008) The RAS/MAPK syndromes: novel roles of the RAS pathway in human genetic disorders Hum. Mutat. 29, 992-1006
6. Dard, N. and Peter, M. (2006) Scaffold proteins in MAP kinase signaling: more than simple passive activating platforms Bioessays. 28, 146-156
7. McKay, M. M. and Morrison, D. K. (2007) Integrating signals from RTKs to ERK//MAPK Oncogene 26, 3113-3121
8. Schaeffer, H. J., Catling, A. D., Eblen, S. T., Collier, L. S., Krauss, A., and Weber, M. J. (1998) MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade Science 281, 1668-1671 (Pubitemid 28435581)
9. Michaud, N. R., Therrien, M., Cacace, A., Edsall, L. C., Spiegel, S., Rubin, G. M., and Morrison, D. K. (1997) KSR stimulates Raf-1 activity in a kinase-independent manner Proc. Natl. Acad. Sci U.S.A. 94, 12792-12796 (Pubitemid 27518430)
10. Kolch, W. (2005) Coordinating ERK/MAPK signalling through scaffolds and inhibitors Nat. Rev. Mol. Cell Biol. 6, 827-837 (Pubitemid 41568732)
11. Wunderlich, W., Fialka, I., Teis, D., Alpi, A., Pfeifer, A., Parton, R. G., Lottspeich, F., and Huber, L. A. (2001) A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment J. Cell Biol. 152, 765-776 (Pubitemid 34280161)
12. Teis, D., Wunderlich, W., and Huber, L. A. (2002) Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction Dev. Cell 3, 803-814 (Pubitemid 35460781)
13. Kurzbauer, R., Teis, D., de Araujo, M. E., Maurer-Stroh, S., Eisenhaber, F., Bourenkov, G. P., Bartunik, H. D., Hekman, M., Rapp, U. R., Huber, L. A., and Clausen, T. (2004) Crystal structure of the p14/MP1 scaffolding complex: how a twin couple attaches mitogen-activated protein kinase signaling to late endosomes Proc. Natl. Acad. Sci. U.S.A. 101, 10984-10989 (Pubitemid 38989571)
14. Lunin, V. V., Munger, C., Wagner, J., Ye, Z., Cygler, M., and Sacher, M. (2004) The structure of the MAP kinase scaffold MP1 bound to its partner p14: a complex with a critical role in endosomal MAP kinase signaling J. Biol. Chem. 279, 23422-23430 (Pubitemid 38685652)
15. Nada, S., Hondo, A., Kasai, A., Koike, M., Saito, K., Uchiyama, Y., and Okada, M. (2009) The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes EMBO J. 28, 477-489
16. Martin, B. R. and Cravatt, B. F. (2009) Large-scale profiling of protein palmitoylation in mammalian cells Nature Methods 6, 135-138
17. Teis, D., Taub, N., Kurzbauer, R., Hilber, D., de Araujo, M. E., Erlacher, M., Offterdinger, M., Villunger, A., Geley, S., Bohn, G., Klein, C., Hess, M. W., and Huber, L. A. (2006) p14-MP1-MEK1 signaling regulates endosomal traffic and cellular proliferation during tissue homeostasis J. Cell Biol. 175, 861-868 (Pubitemid 44969192)
18. Guillaumot, P., Luquain, C., Malek, M., Huber, A. L., Brugiere, S., Garin, J., Grunwald, D., Regnier, D., Petrilli, V., Lefai, E., and Manie, S. N. (2010) Pdro, a protein associated with late endosomes and lysosomes and implicated in cellular cholesterol homeostasis PLoS ONE 5, e10977
19. Hoshino, D., Tomari, T., Nagano, M., Koshikawa, N., and Seiki, M. (2009) A novel protein associated with membrane-type 1 matrix metalloproteinase binds p27(kip1) and regulates RhoA activation, actin remodeling, and matrigel invasion J. Biol. Chem. 284, 27315-27326
20. Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., and Sabatini, D. M. (2010) Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids Cell 141, 290-303
21. Bryson, K., McGuffin, L. J., Marsden, R. L., Ward, J. J., Sodhi, J. S., and Jones, D. T. (2005) Protein structure prediction servers at University College London Nucleic Acids Res. 33, W36-W38
22. Apweiler, R., Attwood, T. K., Bairoch, A., Bateman, A., Birney, E., Biswas, M., Bucher, P., Cerutti, L., Corpet, F., Croning, M. D., Durbin, R., Falquet, L., Fleischmann, W., Gouzy, J., Hermjakob, H., Hulo, N., Jonassen, I., Kahn, D., Kanapin, A., Karavidopoulou, Y., Lopez, R., Marx, B., Mulder, N. J., Oinn, T. M., Pagni, M., Servant, F., Sigrist, C. J., and Zdobnov, E. M. (2001) The InterPro database, an integrated documentation resource for protein families, domains and functional sites Nucleic Acids Res. 29, 37-40 (Pubitemid 32054401)
23. Vincentelli, R., Canaan, S., Campanacci, V., Valencia, C., Maurin, D., Frassinetti, F., Scappucini-Calvo, L., Bourne, Y., Cambillau, C., and Bignon, C. (2004) High-throughput automated refolding screening of inclusion bodies Protein Sci. 13, 2782-2792 (Pubitemid 39274645)
24. Chiu, J., March, P. E., Lee, R., and Tillett, D. (2004) Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h Nucleic Acids Res. 32, e174
25. Magnusdottir, A., Johansson, I., Dahlgren, L. G., Nordlund, P., and Berglund, H. (2009) Enabling IMAC purification of low abundance recombinant proteins from E. coli lysates Nature Methods 6, 477-478
26. Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics Protein Sci. 11, 739-756 (Pubitemid 34241284)
27. Groemping, Y. and Hellmann, N. (2005) (Coligan, J. E., Dunn, B. M., Speicher, D. W., and Wingfield, P. T., Eds.) John Wiley & Sons, Inc., Hoboken, NJ.
28. Russo, A. A., Jeffrey, P. D., Patten, A. K., Massague, J., and Pavletich, N. P. (1996) Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex Nature 382, 325-331 (Pubitemid 26260452)
29. Lacy, E. R., Filippov, I., Lewis, W. S., Otieno, S., Xiao, L., Weiss, S., Hengst, L., and Kriwacki, R. W. (2004) p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding Nat. Struct. Mol. Biol. 11, 358-364 (Pubitemid 38436801)