Chapter 14

Where to Start

Scott, J. D., and Pawson, T. 2000. Cell communication: The inside story. Sci. Am. 282(6):7279.

Pawson, T. 1995. Protein modules and signalling networks. Nature 373:573–580.

B14

Okada, T., Ernst, O. P., Palczewski, K., and Hofmann, K. P. 2001. Activation of rhodopsin: New insights from structural and biochemical studies. Trends Biochem. Sci. 26:318–324.

Tsien, R. Y. 1992. Intracellular signal transduction in four dimensions: From molecular design to physiology. Am. J. Physiol. 263: C723–C728.

Loewenstein, W. R. 1999. Touchstone of Life: Molecular Information, Cell Communication, and the Foundations of Life. Oxford University Press.

G Proteins and 7TM Receptors

Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Le Trong, I., Teller, D. C., Okada, T., Stenkamp, R. E., et al. 2000. Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289:739–745.

Rasmussen, S. G. F., Choi, H.-J., Rosenbaum, D. M., Kobilka, T. S., Thian, F. S., Edwards, P. C., Burghammer, M., Ratnala, V. R. P., Sanishvili, R., Fischetti, R. F., et al. 2007. Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature 450:383–387.

Rosenbaum, D. M., Cherezov, V., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H.-J., Yao, X.-J., Weis, W. I., Stevens, R. C., et al. 2007. GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function. Science 318:1266–1273.

Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. 2011. Crystal structure of the β2 adrenergic receptor–Gs protein complex. Nature 477:549–555.

Lefkowitz, R. J. 2000. The superfamily of heptahelical receptors. Nat. Cell Biol. 2:E133–E136.

Audet, M., and Bouvier, M. 2012. Restructuring G-protein-coupled receptor activation. Cell 151:14–22.

Bourne, H. R., Sanders, D. A., and McCormick, F. 1991. The GTPase superfamily: Conserved structure and molecular mechanism. Nature 349:117–127.

Lambright, D. G., Noel, J. P., Hamm, H. E., and Sigler, P. B. 1994. Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 369:621–628.

Noel, J. P., Hamm, H. E., and Sigler, P. B. 1993. The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366: 654–663.

Sondek, J., Lambright, D. G., Noel, J. P., Hamm, H. E., and Sigler, P. B. 1994. GTPase mechanism of G proteins from the 1.7-Å crystal structure of transducin α-GDP-AIF4. Nature 372:276–279.

Sondek, J., Bohm, A., Lambright, D. G., Hamm, H. E., and Sigler, P. B. 1996. Crystal structure of a G-protein βγ dimer at 2.1 Å resolution. Nature 379:369–374.

Wedegaertner, P. B., Wilson, P. T., and Bourne, H. R. 1995. Lipid modifications of trimeric G proteins. J. Biol. Chem. 270: 503–506.

Farfel, Z., Bourne, H. R., and Iiri, T. 1999. The expanding spectrum of G protein diseases. New Engl. J. Med. 340:1012–1020.

Bockaert, J., and Pin, J. P. 1999. Molecular tinkering of G protein-coupled receptors: An evolutionary success. EMBO J. 18: 1723–1729.

Cyclic AMP Cascade

Hurley, J. H. 1999. Structure, mechanism, and regulation of mammalian adenylyl cyclase. J. Biol. Chem. 274:7599–7602.

Kim, C., Xuong, N. H., and Taylor, S. S. 2005. Crystal structure of a complex between the catalytic and regulatory (RI) subunits of PKA. Science 307:690–696.

Tesmer, J. J., Sunahara, R. K., Gilman, A. G., and Sprang, S. R. 1997. Crystal structure of the catalytic domains of adenylyl cyclase in a complex with G-GTPγS. Science 278:1907–1916.

Smith, C. M., Radzio-Andzelm, E., Madhusudan, Akamine, P., and Taylor, S. S. 1999. The catalytic subunit of cAMP-dependent protein kinase: Prototype for an extended network of communication. Prog. Biophys. Mol. Biol. 71:313–341.

Taylor, S. S., Buechler, J. A., and Yonemoto, W. 1990. cAMP-dependent protein kinase: Framework for a diverse family of regulatory enzymes. Annu. Rev. Biochem. 59:971–1005.

Phosphoinositide Cascade

Berridge, M. J., and Irvine, R. F. 1989. Inositol phosphates and cell signalling. Nature 341:197–205.

Berridge, M. J. 1993. Inositol trisphosphate and calcium signalling. Nature 361:315–325.

Essen, L. O., Perisic, O., Cheung, R., Katan, M., and Williams, R. L. 1996. Crystal structure of a mammalian phosphoinositide-specific phospholipase C δ. Nature 380:595–602.

Ferguson, K. M., Lemmon, M. A., Schlessinger, J., and Sigler, P. B. 1995. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83:1037–1046.

Baraldi, E., Carugo, K. D., Hyvonen, M., Surdo, P. L., Riley, A. M., Potter, B. V., O’Brien, R., Ladbury, J. E., and Saraste, M. 1999. Structure of the PH domain from Bruton’s tyrosine kinase in complex with inositol 1,3,4,5-tetrakisphosphate. Struct. Fold. Design 7:449–460.

Waldo, G. L., Ricks, T. K., Hicks, S. N., Cheever, M. L., Kawano, T., Tsuboi, K., Wang, X., Montell, C., Kozasa, T., Sondek, J., et al. 2010. Kinetic scaffolding mediated by a phospholipase C-β and Gq signaling complex. Science 330:974–980.

Calcium

Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B., and Bax, A. 1992. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256:632–638.

Kuboniwa, H., Tjandra, N., Grzesiek, S., Ren, H., Klee, C. B., and Bax, A. 1995. Solution structure of calcium-free calmodulin. Nat. Struct. Biol. 2:768–776.

Grynkiewicz, G., Poenie, M., and Tsien, R. Y. 1985. A new generation of Ca2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 260:3440–3450.

Kerr, R., Lev-Ram, V., Baird, G., Vincent, P., Tsien, R. Y., and Schafer, W. R. 2000. Optical imaging of calcium transients in neurons and pharyngeal muscle of C. elegans. Neuron 26:583–594.

Chin, D., and Means, A. R. 2000. Calmodulin: A prototypical calcium sensor. Trends Cell Biol. 10:322–328.

Dawson, A. P. 1997. Calcium signalling: How do IP3 receptors work? Curr. Biol. 7:R544–R547.

Protein Kinases, Including Receptor Tyrosine Kinases

Riedel, H., Dull, T. J., Honegger, A. M., Schlessinger, J., and Ullrich, A. 1989. Cytoplasmic domains determine signal specificity, cellular routing characteristics and influence ligand binding of epidermal growth factor and insulin receptors. EMBO J. 8:2943–2954.

Taylor, S. S., Knighton, D. R., Zheng, J., Sowadski, J. M., Gibbs, C. S., and Zoller, M. J. 1993. A template for the protein kinase family. Trends Biochem. Sci. 18:84–89.

Sicheri, F., Moarefi, I., and Kuriyan, J. 1997. Crystal structure of the Src family tyrosine kinase Hck. Nature 385:602–609.

Waksman, G., Shoelson, S. E., Pant, N., Cowburn, D., and Kuriyan, J. 1993. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms. Cell 72:779–790.

Schlessinger, J. 2000. Cell signaling by receptor tyrosine kinases. Cell 103:211–225.

Simon, M. A. 2000. Receptor tyrosine kinases: Specific outcomes from general signals. Cell 103:13–15.

B15

Robinson, D. R., Wu, Y. M., and Lin, S. F. 2000. The protein tyrosine kinase family of the human genome. Oncogene 19:5548–5557.

Hubbard, S. R. 1999. Structural analysis of receptor tyrosine kinases. Prog. Biophys. Mol. Biol. 71:343–358.

Carter-Su, C., and Smit, L. S. 1998. Signaling via JAK tyrosine kinases: Growth hormone receptor as a model system. Recent Prog. Horm. Res. 53:61–82.

Insulin Signaling Pathway

Khan, A. H., and Pessin, J. E. 2002. Insulin regulation of glucose uptake: A complex interplay of intracellular signalling pathways. Diabetologia 45:1475–1483.

Bevan, P. 2001. Insulin signalling. J. Cell Sci. 114:1429–1430.

De Meyts, P., and Whittaker, J. 2002. Structural biology of insulin and IGF1 receptors: Implications for drug design. Nat. Rev. Drug Discov. 1:769–783.

Dhe-Paganon, S., Ottinger, E. A., Nolte, R. T., Eck, M. J., and Shoelson, S. E. 1999. Crystal structure of the pleckstrin homology-phosphotyrosine binding (PH-PTB) targeting region of insulin receptor substrate 1. Proc. Natl. Acad. Sci. U.S.A. 96:8378–8383.

Domin, J., and Waterfield, M. D. 1997. Using structure to define the function of phosphoinositide 3-kinase family members. FEBS Lett. 410:91–95.

Hubbard, S. R. 1997. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16:5572–5581.

Hubbard, S. R., Wei, L., Ellis, L., and Hendrickson, W. A. 1994. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372:746–754.

EGF Signaling Pathway

Burgess, A. W., Cho, H. S., Eigenbrot, C., Ferguson, K. M., Garrett, T. P., Leahy, D. J., Lemmon, M. A., Sliwkowski, M. X., Ward, C. W., and Yokoyama, S. 2003. An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol. Cell 12:541–552.

Cho, H. S., Mason, K., Ramyar, K. X., Stanley, A. M., Gabelli, S. B., Denney, D. W., Jr., and Leahy, D. J. 2003. Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature 421:756–760.

Chong, H., Vikis, H. G., and Guan, K. L. 2003. Mechanisms of regulating the Raf kinase family. Cell. Signal. 15:463–469.

Stamos, J., Sliwkowski, M. X., and Eigenbrot, C. 2002. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J. Biol. Chem. 277:46265–46272.

Ras

Milburn, M. V., Tong, L., deVos, A. M., Brunger, A., Yamaizumi, Z., Nishimura, S., and Kim, S. H. 1990. Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic Ras proteins. Science 247:939–945.

Boriack-Sjodin, P. A., Margarit, S. M., Bar-Sagi, D., and Kuriyan, J. 1998. The structural basis of the activation of Ras by Sos. Nature 394:337–343.

Maignan, S., Guilloteau, J. P., Fromage, N., Arnoux, B., Becquart, J., and Ducruix, A. 1995. Crystal structure of the mammalian Grb2 adaptor. Science 268:291–293.

Takai, Y., Sasaki, T., and Matozaki, T. 2001. Small GTP-binding proteins. Physiol. Rev. 81:153–208.

Cancer

Druker, B. J., Sawyers, C. L., Kantarjian, H., Resta, D. J., Reese, S. F., Ford, J. M., Capdeville, R., and Talpaz, M. 2001. Activity of a specific inhibitor of the BCR-ABL tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome. New Engl. J. Med. 344:1038–1042.

Vogelstein, B., and Kinzler, K. W. 1993. The multistep nature of cancer. Trends Genet. 9:138–141.

Ellis, C. A., and Clark, G. 2000. The importance of being K-Ras. Cell. Signal. 12:425–434.

Hanahan, D., and Weinberg, R. A. 2000. The hallmarks of cancer. Cell 100:57–70.

McCormick, F. 1999. Signalling networks that cause cancer. Trends Cell Biol. 9:M53–M56.