Getting a first clue about SPRED functions

BioEssays

Volumn 29, Issue 9, 2007, Pages 897-907

  Bundschu, Karin ^a,b   Walter, Ulrich ^b   Schuh, Kai ^b,c  

^a UNIVERSITY OF ULM   (Germany)

^b UNIVERSITY HOSPITAL WÜRZBURG   (Germany)

^c UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALLERGEN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN SPRED; RAS PROTEIN; REGULATOR PROTEIN; RHO FACTOR; SPROUTY PROTEIN; STEM CELL FACTOR RECEPTOR; TUMOR MARKER; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

CANCER INHIBITION; CARCINOGENESIS; CELL FUNCTION; CELL MIGRATION; CELL MOTILITY; CELLULAR DISTRIBUTION; DWARFISM; EOSINOPHILIA; GASTRULATION; GENE DISRUPTION; HEMATOPOIESIS; HUMAN; MESODERM; METASTASIS; MITOGENESIS; MORPHOGENESIS; NONHUMAN; OSSIFICATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; REVIEW; XENOPUS;

MUS; VERTEBRATA;

EID: 34548751238     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20632     Document Type: Review

References (70)

1. Wakioka T, Sasaki A, Kato R, Shouda T, Matsumoto A, et al. 2001. Spred is a Sprouty-related suppressor of Ras signalling. Nature 412:647-651.
2. Kato R, Nonami A, Taketomi T, Wakioka T, Kuroiwa A, et al. 2003. Molecular cloning of mammalian Spred-3 which suppresses tyrosine kinase-mediated Erk activation. Biochem Biophys Res Commun 302:767-772.
3. Sivak JM, Petersen LF, Amaya E. 2005. FGF signal interpretation is directed by Sprouty and Spred proteins during mesoderm formation. Dev Cell 8:689-701.
4. DeMille MM, Kimmel BE, Rubin GM. 1996. A Drosophila gene regulated by rough and glass shows similarity to ena and VASP. Gene 183:103-108.
5. Hacohen N, Kramer S, Sutherland D, Hiromi Y, Krasnow MA. 1998. Sprouty encodes a novel antagonist of FGF signalling that patterns apical branching of the Drosophil a airways. Cell 92:253-263.
6. Kim HJ, Bar-Sagi D. 2004. Modulation of signalling by Sprouty: a developing story. Nat Rev Mol Cell Biol 5:441-450.
7. Bundschu K, Knobeloch KP, Ullrich M, Schinke T, Amling M, et al. 2005. Gene disruption of Spred-2 causes dwarfism. J Biol Chem 280:28572-28580.
8. Nobuhisa I, Kato R, Inoue H, Takizawa M, Okita K, et al. 2004. Spred-2 suppresses aorta-gonad-mesonephros hematopoiesis by inhibiting MAP kinase activation. J Exp Med 199:737-742.
9. Inoue H, Kato R, Fukuyama S, Nonami A, Taniguchi K, et al. 2005. Spred-1 negatively regulates allergen-induced airway eosinophilia and hyperresponsiveness. J Exp Med 201:73-82.
10. Miyoshi K, Wakioka T, Nishinakamura H, Kamio M, Yang L, et al. 2004. The Sprouty-related protein, Spred, inhibits cell motility, metastasis, and Rho-mediated actin reorganization. Oncogene 23:5567-5576.
11. Yoshida T, Hisamoto T, Akiba J, Koga H, Nakamura K, et al. 2006. Spreds, inhibitors of the Ras/ERK signal transduction, are dysregulated in human hepatocellular carcinoma and linked to the malignant phenotype of tumors. Oncogene 25:6056-6066.
12. Engelhardt CM, Bundschu K, Messerschmitt M, Renne T, Walter U, et al. 2004. Expression and subcellular localization of Spred proteins in mouse and human tissues. Histochem Cell Biol 122:527-538.
13. King JA, Corcoran NM, D'Abaco GM, Straffon AF, Smith CT, et al. 2006. Eve-3: A liver enriched suppressor of Ras/MAPK signalling. J Hepatol 44:758-767.
14. Ball LJ, Jarchau T, Oschkinat H, Walter U. 2002. EVH1 domains: structure, function and interactions. FEBS Lett 513:45-52.
15. Niebuhr K, Ebel F, Frank R, Reinhard M, Domann E, et al. 1997. A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the EnaA/ASP family. Embo J 16:5433-5444.
16. Reinhard M, Rudiger M, Jockusch BM, Walter U. 1996. VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs. FEBS Lett 399:103-107.
17. Machesky LM, Way M. 1998. Actin branches out. Nature 394:125-126.
18. Reinhard M, Jouvenal K, Tripier D, Walter U. 1995. Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc Natl Acad Sci USA 92:7956-7960.
19. Samarin S, Romero S, Kocks C, Didry D, Pantaloni D, et al. 2003. How VASP enhances actin-based motility. J Cell Biol 163:131-142.
20. Reinhard M, Jarchau T, Walter U. 2001. Actin-based motility: stop and go with Ena/VASP proteins. Trends Biochem Sci 26:243-249.
21. Renfranz PJ, Beckerle MC. 2002. Doing (F/L)PPPPs: EVH1 domains and their proline-rich partners in cell polarity and migration. Curr Opin Cell Biol 14:88-103.
22. Callebaut I, Cossart P, Dehoux P. 1998. EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family. FEBS Lett 441:181-185.
23. Zimmermann J, Jarchau T, Walter U, Oschkinat H, Ball LJ. 2004. 1H, 13C and 15N resonance assignment of the human Spred2 EVH1 domain. J Biomol NMR 29:435-436.
24. Harmer NJ, Sivak JM, Amaya E, Blundell TL. 2005. 1.15 A crystal structure of the X. tropicalis Spred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family. FEBS Lett 579:1161-1166.
25. King JA, Straffon AF, D'Abaco GM, Poon CL, I ST, et al. 2005. Distinct requirements for the Sprouty domain for functional activity of Spred proteins. Biochem J 388:445-454.
26. Nonami A, Kato R, Taniguchi K, Yoshiga D, Taketomi T, et al. 2004. Spred-1 negatively regulates interleukin-3-mediated ERK/MAP kinase activation in hematopoietic cells. J Biol Chem 279:52543-52551.
27. Kramer S, Okabe M, Hacohen N, Krasnow MA, Hiromi Y. 1999. Sprouty: a common antagonist of FGF and EGF signalling pathways in Drosophila. Development 126:2515-2525.
28. Reich A, Sapir A, Shilo B. 1999. Sprouty is a general inhibitor of receptor tyrosine kinase signalling. Development 126:4139-4147
29. Sasaki A, Taketomi T, Kato R, Saeki K, Nonami A, et al. 2003. Mammalian Sprouty4 suppresses Ras-independent ERK activation by binding to Raf1. Nat Cell Biol 5:427-432.
30. Lim J, Yusoff P, Wong ES, Chandramouli S, Lao DH, et al. 2002. The cysteine-rich sprouty translocation domain targets mitogen-activated protein kinase inhibitory proteins to phosphatidylinositol 4,5-bisphosphate in plasma membranes. Mol Cell Biol 22:7953-7966.
31. Nonami A, Taketomi T, Kimura A, Saeki K, Takaki H, et al. 2005. The Sprouty-related protein, Spred-1, localizes in a lipid raft/caveola and inhibits ERK activation in collaboration with caveolin-1. Genes Cells 10:887-895.
32. Harris J, Werling D, Hope JC, Taylor G, Howard CJ. 2002. Caveolae and caveolin in immune cells: distribution and functions. Trends Immunol 23:158-164.
33. Engelhardt CM, Bundschu K, Messerschmitt M, Renne T, Walter U, et al. 2004. Expression and subcellular localization of Spred proteins in mouse and human tissues. Histochem Cell Biol 122:527-538.
34. Bundschu K, Gattenlohner S, Knobeloch KP, Walter U, Schuh K. 2006. Tissue-specific Spred-2 promoter activity characterized by a gene trap approach. Gene Expr Patterns 6:247-255.
35. Chen W, Feng Y, Chen D, Wandinger-Ness A. 1998. Rab11 is required for trans-golgi network-to-plasma membrane transport and a preferential target for GDP dissociation inhibitor. Mol Biol Cell 9:3241-3257.
36. Sonnichsen B, De Renzis S, Nielsen E, Rietdorf J, Zerial M. 2000. Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J Cell Biol 149:901-914.
37. Ullrich O, Reinsch S, Urbe S, Zerial M, Parton RG. 1996. Rab11 regulates recycling through the pericentriolar recycling endosome. J Cell Biol 135:913-924.
38. Hashimoto S, Nakano H, Singh G, Katyal S. 2002. Expression of Spred and Sprouty in developing rat lung. Mech Dev 119 (Suppl 1):S303-S309.
39. Lock P, I ST, Straffon AF, Schieb H, Hovens CM, et al. 2006. Spred-2 steady-state levels are regulated by phosphorylation and Cbl-mediated ubiquitination. Biochem Biophys Res Commun 351:1018-1023.
40. Lowy DR, Willumsen BM. 1993. Function and regulation of ras. Annu Rev Biochem 62:851-891.
41. Morrison DK, Cutler RE. 1997. The complexity of Raf-1 regulation. Curr Opin Cell Biol 9:174-179.
42. Sternberg PW, Alberola-Ila J. 1998. Conspiracy theory: RAS and RAF do not act alone. Cell 95:447-450.
43. Kerkhoff E, Rapp UR. 2001. The Ras-Raf relationship: an unfinished puzzle. Adv Enzyme Regul 41:261-267.
44. Gille H, Kortenjann M, Thomae O, Moomaw C, Slaughter C, et al. 1995. ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. Embo J 14:951-962.
45. York RD, Yao H, Dillon T, Ellig CL, Eckert SP, et al. 1998. Rap1 mediates sustained MAP kinase activation induced by nerve growth factor. Nature 392:622-626.
46. Kao S, Jaiswal RK, Kolch W, Landreth GE. 2001. Identification of the mechanisms regulating the differential activation of the mapk cascade by epidermal growth factor and nerve growth factor in PC12 cells. J Biol Chem 276:18169-18177.
47. Nutt SL, Dingwell KS, Holt CE, Amaya E. 2001. Xenopus Sprouty2 inhibits FGF-mediated gastrulation movements but does not affect mesoderm induction and patterning. Genes Dev 15:1152-1166.
48. Impagnatiello MA, Weitzer S, Gannon G, Compagni A, Cotten M, et al. 2001. Mammalian sprouty-1 and -2 are membrane-anchored phosphoprotein inhibitors of growth factor signaling in endothelial cells. J Cell Biol 152:1087-1098.
49. Ridley AJ, Hall A. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
50. Izawa I, Amano M, Chihara K, Yamamoto T, Kaibuchi K. 1998. Possible involvement of the inactivation of the Rho-Rho-kinase pathway in oncogenic Ras-induced transformation. Oncogene 17:2863-2871.
51. Lo TL, Yusoff P, Fong CW, Guo K, McCaw BJ et al. 2004. The ras/mitogen-activated protein kinase pathway inhibitor and likely tumor suppressor proteins, sprouty 1 and sprouty 2 are deregulated in breast cancer. Cancer Res 64:6127-6136.
52. Kwabi-Addo B, Ozen M, Ittmann M. 2004. The role of fibroblast growth factors and their receptors in prostate cancer. Endocr Relat Cancer 11:709-724.
53. McKie AB, Douglas DA, Olijslagers S, Graham J, Omar MM, et al. 2005. Epigenetic inactivation of the human sprouty2 (hSPRY2) homologue in prostate cancer. Oncogene 24:2166-2174.
54. Wang J, Thompson B, Ren C, Ittmann M, Kwabi-Addo B. 2006. Sprouty4, a suppressor of tumor cell motility, is downregulated by DNA methylation in human prostate cancer. Prostate 66:613-624.
55. Tsavachidou D, Coleman ML, Athanasiadis G, Li S, Licht JD, et al. 2004. SPRY2 is an inhibitor of the ras/extracellular signal-regulated kinase pathway in melanocytes and melanoma cells with wild-type BRAF but not with the V599E mutant. Cancer Res 64:5556-5559.
56. Fong CW, Chua MS, McKie AB, Ling SH, Mason V, et al. 2006. Sprouty 2, an inhibitor of mitogen-activated protein kinase signaling, is down-regulated in hepatocellular carcinoma. Cancer Res 66:2048-2058.
57. Lo TL, Fong CW, Yusoff P, McKie AB, Chua MS, et al. 2006. Sprouty and cancer: The first terms report. Cancer Lett 242:141-150.
58. Hogan MB, Weissman DN, Hubbs AF, Gibson LF, Piktel D, et al. 2003. Regulation of eosinophilopoiesis in a murine model of asthma. J Immunol 171:2644-2651.
59. Inman MD, Ellis R, Wattie J, Denburg JA, O'Byrne PM. 1999. Allergen-induced increase in airway responsiveness, airway eosinophilia, and bone-marrow eosinophil progenitors in mice. Am J Respir Cell Mol Biol 21:473-479.
60. Coffin JD, Florkiewicz RZ, Neumann J, Mort-Hopkins T, Dorn GW, 2nd, et al. 1995. Abnormal bone growth and selective translational regulation in basic fibroblast growth factor (FGF-2) transgenic mice. Mol Biol Cell 6:1861-1873.
61. Garofalo S, Kliger-Spatz M, Cooke JL, Wolstin O, Lunstrum GP, et al. 1999. Skeletal dysplasia and defective chondrocyte differentiation by targeted overexpression of fibroblast growth factor 9 in transgenic mice. J Bone Miner Res 14:1909-1915.
62. Naski MC, Ornitz DM. 1998. FGF signaling in skeletal development. Front Biosci 3:D781-794.
63. Li C, Chen L, Iwata T, Kitagawa M, Fu XY, et al. 1999. A Lys644Glu substitution in fibroblast growth factor receptor 3 (FGFR3) causes dwarfism in mice by activation of STATs and ink4 cell cycle inhibitors. Hum Mol Genet 8:35-44.
64. Wang Y, Spatz MK, Kannan K, Hayk H, Avivi A, et al. 1999. A mouse model for achondroplasia produced by targeting fibroblast growth factor receptor 3. Proc Natl Acad Sci USA 96:4455-4460.
65. Iwata T, Chen L, Li C, Ovchinnikov DA, Behringer RR, et al. 2000. A neonatal lethal mutation in FGFR3 uncouples proliferation and differentiation of growth plate chondrocytes in embryos. Hum Mol Genet 9:1603-1613.
66. Iwata T, Li CL, Deng CX, Francomano CA. 2001. Highly activated Fgfr3 with the K644M mutation causes prolonged survival in severe dwarf mice. Hum Mol Genet 10:1255-1264.
67. Segev O, Chumakov I, Nevo Z, Givol D, Madar-Shapiro L, et al. 2000. Restrained chondrocyte proliferation and maturation with abnormal growth plate vascularization and ossification in human FGFR-3(G380R) transgenic mice. Hum Mol Genet 9:249-258.
68. Chen L, Li C, Qiao W, Xu X, Deng C. 2001. A Ser(365)→Cys mutation of fibroblast growth factor receptor 3 in mouse downregulates Ihh/PTHrP signals and causes severe achondroplasia. Hum Mol Genet 10:457-465.
69. Murakami S, Balmes G, McKinney S, Zhang Z, Givol D, et al. 2004. Constitutive activation of MEK1 in chondrocytes causes Stat1-independent achondroplasia-like dwarfism and rescues the Fgfr3-deficient mouse phenotype. Genes Dev 18:290-305.
70. Taniguchi K, Kohno RI, Ayada T, Kato R, Ichiyama K, et al. 2007. Spreds are essential for embryonic lymphangiogenesis by regulating vascular endothelial growth factor receptor-3 signalling. Mol Cell Biol.