Signaling in the Endocrine System

Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)


Focal Adhesion Kinase Nonreceptor Tyrosine Kinase Sterile Alpha Motif Sterile Alpha Motif Domain Tyrosine Phosphorylation Site 
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References and Further Reading


  1. Ferrara N, Gerber HP, and LeCouter J [2001]. The biology of VEGF and its receptors. Nature Med., 9: 669–676.CrossRefGoogle Scholar
  2. Gale NW, and Yancopoulos GD [1999]. Growth factors acting via endothelial cellspecific receptor tyrosine kinases: VEGFs, angiopoietins and ephrins in vascular development. Genes Dev., 13: 1055–1066.CrossRefGoogle Scholar
  3. Jones N, et al. [2003]. Tie receptors: New modulators of angiogenic and lymphangiogenic responses. Nature Rev. Mol. Cell Biol. 2: 257–267.CrossRefGoogle Scholar
  4. Neufeld G, et al. [1999]. Vascular endothelial growth factor (VEGF) and its receptors. FASEB J., 13: 9–22.Google Scholar
  5. Yancopoulos GD, et al. [2000]. Vascular-specific growth factors and blood vessel formation. Nature, 407: 242–248.CrossRefGoogle Scholar


  1. Chao MV [2003]. Neurotrophins and their receptors: A convergence point for many signaling pathways. Nature Rev. Neurosci., 4: 299–309.CrossRefGoogle Scholar
  2. Lee R, et al. [2001]. Regulation of cell survival by secreted proneurotrophins. Science, 294: 1945–1948.CrossRefADSGoogle Scholar
  3. Zheng YZ, et al. [2000]. Cell surface Trk receptors mediate NFG-induced survival while internalized receptors regulate NFG-induced differentiation. J. Neurosci., 20: 5671–5678.Google Scholar

Ligand-Induced, Receptor-Mediated Dimerization

  1. Schlessinger J [2002]. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell, 110: 669–672.CrossRefGoogle Scholar

Phosphoprotein Recognition

  1. Berg D, Holzmann C, and Reiss O [2003]. 14-3-3 proteins in the nervous system. Nature Rev. Neurosci., 4: 752–762.CrossRefGoogle Scholar
  2. Durocher D, and Jackson SP [2002]. The FHA domain. FEBS Lett., 513: 58–66.CrossRefGoogle Scholar
  3. Forman-Kay JD, and Pawson T [1999]. Diversity in protein recognition by PTB domains. Curr. Opin. Struct. Biol., 9: 690–695.CrossRefGoogle Scholar
  4. Pawson T, Gish GD, and Nash P [2001]. SH2 domain, interaction modules and cellular wiring. Trends Cell Biol., 11: 504–511.CrossRefGoogle Scholar
  5. Tzivion G, and Avruch J [2002]. 14-3-3 proteins: Active cofactors in cellular regulation by serine/threonine phosphorylation. J. Biol. Chem., 277: 3061–3064.CrossRefGoogle Scholar
  6. Yaffe MB [2002]. Phosphotyrosine-binding domains in signal transduction. Nature Rev. Mol. Cell Biol., 3: 177–186.CrossRefGoogle Scholar

Recognition of Proline-Rich Motifs

  1. Ball LJ, et al. [2002]. EVH1 domains: Structure, function and interactions. FEBS Lett., 513: 45–52.CrossRefGoogle Scholar
  2. Freund C, et al. [1999]. The GYF domain is a novel structural fold that is involved in lymphoid signaling through praline-rich sequences. Nature Struct. Biol., 6: 656–660.CrossRefGoogle Scholar
  3. Kay BK, Williamson MP, 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.Google Scholar
  4. Macias MJ, Wiesner S, and Sudol M [2002]. WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett., 513: 30–37.CrossRefGoogle Scholar
  5. Mayer BJ [2001]. SH3 domains: Complexity in moderation. J. Cell Sci., 114: 1253–1263.Google Scholar
  6. Zarrinpar A, and Lim WA [2000]. Converging on proline: The mechanism of WW domain peptide recognition. Nature Struct. Biol., 7: 611–613.CrossRefGoogle Scholar

Protein-Protein Interaction Domains

  1. Aravind L, Dixit MV, and Koonin EV [1999]. The domains of death: evolution of the apoptosis machinery. Trends Biochem. Sci., 24: 47–53.CrossRefGoogle Scholar
  2. Harris BZ, and Lim WA [2001]. Mechanism and role of PDZ domains in signaling complex assembly. J. Cell Sci., 114: 3219–3231.Google Scholar
  3. Hepler JR [1999]. Emerging roles for RGS proteins in cell signaling. Trends Pharmacol. Sci., 20: 376–382.CrossRefGoogle Scholar
  4. Hofmann K [1999]. The modular nature of apoptotic signaling proteins. Cell. Mol. Life Sci., 55: 1113–1128.CrossRefGoogle Scholar
  5. Hung AY, and Sheng M [2002]. PDZ domains: Structural modules for protein complex assembly. J. Biol. Chem., 277: 5699–5702.CrossRefGoogle Scholar
  6. Schultz J, et al. [1997]. SAM as a protein interaction domain involved in developmental regulation. Protein Sci., 6: 249–253.CrossRefGoogle Scholar
  7. Zhong H, and Neubig RR [2001]. Regulator of G protein signaling proteins: Novel multifunctional drug targets. J. Pharmacol. Exp. Ther., 297: 837–845.Google Scholar

Src Nonreceptor Tyrosine Kinase

  1. Brown MT, and Cooper JA [1996]. Regulation, substrates and function of Src. Biochim. Biophys. Acta, 1287: 121–149.Google Scholar
  2. Frame MC, et al. [2002]. v-Src’s hold over actin and cell adhesions. Nature Rev. Mol. Cell Biol., 3: 233–245.MathSciNetCrossRefGoogle Scholar

Focal Adhesions

  1. Ilic D, Damsky CH, and Yamamoto T [1997]. Focal adhesion kinase: At the crossroads of signal transduction. J. Cell Sci., 110: 401–407.Google Scholar
  2. Schlaepfer DD, Hauck CR, and Sieg DJ [1999]. Signaling through focal adhesion kinase. Prog. Biophys. Mol. Biol., 71: 435–478.CrossRefGoogle Scholar
  3. Turner CE [2000]. Paxillin and focal adhesion signaling. Nature Cell Biol., 2: E231–E236.CrossRefGoogle Scholar
  4. Renshaw MW, Ren XD, and Schwartz MA [1997]. Growth factor activation of MAP kinase requires cell adhesion. EMBO J., 16: 5592–5599.CrossRefGoogle Scholar

Ras Family of GTPases

  1. Campbell SL, et al. [1998]. Increasing complexity of Ras signaling. Oncogene, 17: 1395–1413.CrossRefGoogle Scholar
  2. Hancock JF [2003]. Ras proteins: Different signals from different locations. Nature Rev. Mol. Cell Biol., 4: 373–384.CrossRefGoogle Scholar
  3. Kolch W [2000]. Meaningful relationships: The regulation of the Ras/Raf/MEK/ERK pathway by protein interactions. Biochem. J., 351: 289–305.CrossRefGoogle Scholar

Rho Family of GTPases

  1. Gladfelter AS, et al. [2002]. Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p. J. Cell Biol., 156: 315–326.CrossRefGoogle Scholar
  2. Hall A [1998]. Rho GTPases and the actin cytoskeleton. Science, 279: 509–514.CrossRefADSGoogle Scholar
  3. Irazoqui JE, Gladfelter AS, and Lew DJ [2003]. Scaffold mediated symmetry breaking by Cdc42p. Nature Cell Biol., 5: 1062–1070.CrossRefGoogle Scholar
  4. Ren XD, Kiosses WB, and Schwartz MA [1999]. Regulation of the small GTPbinding protein Rho by cell adhesion and the cytoskeleton. EMBO J., 18: 578–585.CrossRefGoogle Scholar
  5. Schwartz MA, and Shattil SJ [2000]. Signaling networks linking integrins and Rho family GTPases. Trends Biochem. Sci., 25: 388–391.CrossRefGoogle Scholar

Ran Family of GTPases

  1. Görlich D, Seawald MJ, and Ribbeck K [2003]. Characterization of Ran-driven cargo transport and the RanGTPase systems by kinetic measurements and computer simulation. EMBO J., 22: 1088–1100.CrossRefGoogle Scholar
  2. Macara IG [2001]. Transport in and out of the nucleus. Microbiol. Mol. Biol. Rev., 65: 570–594.CrossRefGoogle Scholar
  3. Melchior F, and Gerace L [1998]. Two-way trafficking with Ran. Trends Cell Biol., 8: 175–179.CrossRefGoogle Scholar
  4. Weis K [1998]. Importins and exportins: How to get in and out of the nucleus. Trends Biochem. Sci., 23: 185–189.CrossRefGoogle Scholar
  5. Weis K [2003]. Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle. Cell, 112: 441–451.CrossRefGoogle Scholar

Rab and Arf Families of GTPases

  1. Moss J, and Vaughn M [1995]. Structure and function of Arf proteins: Activators of cholera toxin and critical components of intracellular vesicle transport. J. Biol. Chem., 270: 12327–12330.CrossRefGoogle Scholar
  2. Zerial M, and McBride H [2001]. Rab proteins as membrane organizers. Nature Rev. Mol. Cell Biol., 2: 107–117.CrossRefGoogle Scholar

Recycling, and Signaling in the Endocytic Pathway

  1. González-Gaitán M [2003]. Signal dispersal and transduction through the endocytic pathway. Nature Rev. Mol. Cell Biol., 4: 213–224.CrossRefGoogle Scholar
  2. Sorkin A, and von Zastrow M [2002]. Signal transduction and endocytosis: Close encounters of many kinds. Nature Rev. Mol. Cell Biol., 3: 600–614.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, Inc. 2005

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