메뉴 건너뛰기




Volumn 11, Issue 1, 2008, Pages 53-62

Sprouty proteins, masterminds of receptor tyrosine kinase signaling

Author keywords

EGF; Endothelial cell; ERK; FGF; Growth factors; MAPK; Receptor tyrosine kinase; Spred; Sprouty; VEGF

Indexed keywords

EPIDERMAL GROWTH FACTOR; FIBROBLAST GROWTH FACTOR; GROWTH FACTOR; ISOPROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGENIC AGENT; NITRIC OXIDE; PROTEIN TYROSINE KINASE; SPROUTY PROTEIN; VASCULOTROPIN;

EID: 41049103244     PISSN: 09696970     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10456-008-9089-1     Document Type: Review
Times cited : (196)

References (96)
  • 1
    • 2342591455 scopus 로고    scopus 로고
    • The discovery of receptor tyrosine kinases: Targets for cancer therapy
    • Gschwind A, Fischer OM, Ullrich A (2004) The discovery of receptor tyrosine kinases: targets for cancer therapy. Nat Rev Cancer 4:361-370
    • (2004) Nat Rev Cancer , vol.4 , pp. 361-370
    • Gschwind, A.1    Fischer, O.M.2    Ullrich, A.3
  • 2
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA (2000) The hallmarks of cancer. Cell 100:57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 3
    • 30744479430 scopus 로고    scopus 로고
    • Angiogenesis in life, disease and medicine
    • Carmeliet P (2005) Angiogenesis in life, disease and medicine. Nature 438:932-936
    • (2005) Nature , vol.438 , pp. 932-936
    • Carmeliet, P.1
  • 4
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • Hanahan D, Folkman J (1996) Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell 86:353-364
    • (1996) Cell , vol.86 , pp. 353-364
    • Hanahan, D.1    Folkman, J.2
  • 5
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J (2000) Cell signaling by receptor tyrosine kinases. Cell 103:211-225
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 6
    • 0037334338 scopus 로고    scopus 로고
    • Making vascular networks in the adult: Branching morphogenesis without a roadmap
    • Dor Y, Djonov V, Keshet E (2003) Making vascular networks in the adult: branching morphogenesis without a roadmap. Trends Cell Biol 13:131-136
    • (2003) Trends Cell Biol , vol.13 , pp. 131-136
    • Dor, Y.1    Djonov, V.2    Keshet, E.3
  • 7
    • 33845316132 scopus 로고    scopus 로고
    • Comparative mechanisms of branching morphogenesis in diverse systems
    • Lu P, Sternlicht MD, Werb Z (2006) Comparative mechanisms of branching morphogenesis in diverse systems. J Mammary Gland Biol Neoplasia 11:213-228
    • (2006) J Mammary Gland Biol Neoplasia , vol.11 , pp. 213-228
    • Lu, P.1    Sternlicht, M.D.2    Werb, Z.3
  • 8
    • 34249689753 scopus 로고    scopus 로고
    • Molecular regulation of angiogenesis and lymphangiogenesis
    • Adams RH, Alitalo K (2007) Molecular regulation of angiogenesis and lymphangiogenesis. Nat Rev Mol Cell Biol 8:464-478
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 464-478
    • Adams, R.H.1    Alitalo, K.2
  • 9
    • 30744449235 scopus 로고    scopus 로고
    • Angiogenesis as a therapeutic target
    • Ferrara N, Kerbel RS (2005) Angiogenesis as a therapeutic target. Nature 438:967-974
    • (2005) Nature , vol.438 , pp. 967-974
    • Ferrara, N.1    Kerbel, R.S.2
  • 11
    • 34248575149 scopus 로고    scopus 로고
    • Integrating signals from RTKs to ERK/MAPK
    • McKay MM, Morrison DK (2007) Integrating signals from RTKs to ERK/MAPK. Oncogene 26:3113-3121
    • (2007) Oncogene , vol.26 , pp. 3113-3121
    • McKay, M.M.1    Morrison, D.K.2
  • 12
    • 34047174559 scopus 로고    scopus 로고
    • A module of negative feedback regulators defines growth factor signaling
    • Amit I, Citri A, Shay T et al (2007) A module of negative feedback regulators defines growth factor signaling. Nat Genet 39:503-512
    • (2007) Nat Genet , vol.39 , pp. 503-512
    • Amit, I.1    Citri, A.2    Shay, T.3
  • 13
    • 0032559228 scopus 로고    scopus 로고
    • Sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways
    • Hacohen N, Kramer S, Sutherland D et al (1998) sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways. Cell 92:253-263
    • (1998) Cell , vol.92 , pp. 253-263
    • Hacohen, N.1    Kramer, S.2    Sutherland, D.3
  • 14
    • 33845987501 scopus 로고    scopus 로고
    • The VASP-Spred-Sprouty domain puzzle
    • Bundschu K, Walter U, Schuh K (2006) The VASP-Spred-Sprouty domain puzzle. J Biol Chem 281:36477-36481
    • (2006) J Biol Chem , vol.281 , pp. 36477-36481
    • Bundschu, K.1    Walter, U.2    Schuh, K.3
  • 15
    • 0142061026 scopus 로고    scopus 로고
    • Sprouty proteins: Antagonists of endothelial cell signaling and more
    • Cabrita MA, Christofori G (2003) Sprouty proteins: antagonists of endothelial cell signaling and more. Thromb Haemost 90:586-590
    • (2003) Thromb Haemost , vol.90 , pp. 586-590
    • Cabrita, M.A.1    Christofori, G.2
  • 16
    • 0042386618 scopus 로고    scopus 로고
    • Sprouty: How does the branch manager work?
    • Guy GR, Wong ES, Yusoff P et al (2003) Sprouty: how does the branch manager work? J Cell Sci 16:3061-3068
    • (2003) J Cell Sci , vol.16 , pp. 3061-3068
    • Guy, G.R.1    Wong, E.S.2    Yusoff, P.3
  • 17
    • 2942568167 scopus 로고    scopus 로고
    • Modulation of signalling by Sprouty: A developing story
    • Kim HJ, Bar-Sagi D (2004) Modulation of signalling by Sprouty: a developing story. Nat Rev Mol Cell Biol 5:441-450
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 441-450
    • Kim, H.J.1    Bar-Sagi, D.2
  • 18
    • 30444441147 scopus 로고    scopus 로고
    • Sprouty proteins: Multifaceted negative-feedback regulators of receptor tyrosine kinase signaling
    • Mason JM, Morrison DJ, Basson MA et al (2006) Sprouty proteins: multifaceted negative-feedback regulators of receptor tyrosine kinase signaling. Trends Cell Biol 16:45-54
    • (2006) Trends Cell Biol , vol.16 , pp. 45-54
    • Mason, J.M.1    Morrison, D.J.2    Basson, M.A.3
  • 19
    • 34548751238 scopus 로고    scopus 로고
    • Getting a first clue about SPRED functions
    • Bundschu K, Walter U, Schuh K (2007) Getting a first clue about SPRED functions. Bioessays 29:897-907
    • (2007) Bioessays , vol.29 , pp. 897-907
    • Bundschu, K.1    Walter, U.2    Schuh, K.3
  • 20
    • 0036105451 scopus 로고    scopus 로고
    • Human sprouty 4, a new ras antagonist on 5q31, interacts with the dual specificity kinase TESK1
    • Leeksma OC, Van Achterberg TA, Tsumura Y et al (2002) Human sprouty 4, a new ras antagonist on 5q31, interacts with the dual specificity kinase TESK1. Eur J Biochem 269:2546-2556
    • (2002) Eur J Biochem , vol.269 , pp. 2546-2556
    • Leeksma, O.C.1    Van Achterberg, T.A.2    Tsumura, Y.3
  • 21
    • 0032719944 scopus 로고    scopus 로고
    • Vertebrate Sprouty genes are induced by FGF signaling and can cause chondrodysplasia when overexpressed
    • Minowada G, Jarvis LA, Chi CL et al (1999) Vertebrate Sprouty genes are induced by FGF signaling and can cause chondrodysplasia when overexpressed. Development 126:4465-4475
    • (1999) Development , vol.126 , pp. 4465-4475
    • Minowada, G.1    Jarvis, L.A.2    Chi, C.L.3
  • 22
    • 0035824694 scopus 로고    scopus 로고
    • Mammalian sprouty proteins inhibit cell growth and differentiation by preventing ras activation
    • Gross I, Bassit B, Benezra M et al (2001) Mammalian sprouty proteins inhibit cell growth and differentiation by preventing ras activation. J Biol Chem 276:46460-46468
    • (2001) J Biol Chem , vol.276 , pp. 46460-46468
    • Gross, I.1    Bassit, B.2    Benezra, M.3
  • 23
    • 0035809919 scopus 로고    scopus 로고
    • Mammalian sprouty-1 and -2 are membrane-anchored phosphoprotein inhibitors of growth factor signaling in endothelial cells
    • Impagnatiello MA, Weitzer S, Gannon G 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
    • (2001) J Cell Biol , vol.152 , pp. 1087-1098
    • Impagnatiello, M.A.1    Weitzer, S.2    Gannon, G.3
  • 24
    • 0035965203 scopus 로고    scopus 로고
    • Identification of a dominant negative mutant of Sprouty that potentiates fibroblast growth factor- but not epidermal growth factor-induced ERK activation
    • Sasaki A, Taketomi T, Wakioka T et al (2001) Identification of a dominant negative mutant of Sprouty that potentiates fibroblast growth factor- but not epidermal growth factor-induced ERK activation. J Biol Chem 276:36804-36808
    • (2001) J Biol Chem , vol.276 , pp. 36804-36808
    • Sasaki, A.1    Taketomi, T.2    Wakioka, T.3
  • 25
    • 0034693130 scopus 로고    scopus 로고
    • Sprouty proteins are targeted to membrane ruffles upon growth factor receptor tyrosine kinase activation
    • Lim J, Wong ES, Ong SH et al (2000) Sprouty proteins are targeted to membrane ruffles upon growth factor receptor tyrosine kinase activation. Identification of a novel translocation domain. J Biol Chem 275:32837-32845
    • (2000) J Biol Chem , vol.275 , pp. 32837-32845
    • Lim, J.1    Wong, E.S.2    Ong, S.H.3
  • 26
    • 0035933734 scopus 로고    scopus 로고
    • The C terminus of sprouty is important for modulation of cellular migration and proliferation
    • Yigzaw Y, Cartin L, Pierre S et al (2001) The C terminus of sprouty is important for modulation of cellular migration and proliferation. J Biol Chem 276:22742-22747
    • (2001) J Biol Chem , vol.276 , pp. 22742-22747
    • Yigzaw, Y.1    Cartin, L.2    Pierre, S.3
  • 27
    • 19944430510 scopus 로고    scopus 로고
    • Sprouty1 is a critical regulator of GDNF/RET-mediated kidney induction
    • Basson MA, Akbulut S, Watson-Johnson J et al (2005) Sprouty1 is a critical regulator of GDNF/RET-mediated kidney induction. Dev Cell 8:229-239
    • (2005) Dev Cell , vol.8 , pp. 229-239
    • Basson, M.A.1    Akbulut, S.2    Watson-Johnson, J.3
  • 28
    • 34548721613 scopus 로고    scopus 로고
    • Sprouty2 inhibits BDNF-induced signaling and modulates neuronal differentiation and survival
    • Gross I, Armant O, Benosman S et al (2007) Sprouty2 inhibits BDNF-induced signaling and modulates neuronal differentiation and survival. Cell Death Differ 14:1802-1812
    • (2007) Cell Death Differ , vol.14 , pp. 1802-1812
    • Gross, I.1    Armant, O.2    Benosman, S.3
  • 29
    • 3142736728 scopus 로고    scopus 로고
    • Overexpression of sprouty 2 inhibits HGF/SF-mediated cell growth, invasion, migration, and cytokinesis
    • Lee CC, Putnam AJ, Miranti CK et al (2004) Overexpression of sprouty 2 inhibits HGF/SF-mediated cell growth, invasion, migration, and cytokinesis. Oncogene 23:5193-5202
    • (2004) Oncogene , vol.23 , pp. 5193-5202
    • Lee, C.C.1    Putnam, A.J.2    Miranti, C.K.3
  • 30
    • 33646488029 scopus 로고    scopus 로고
    • Dual effects of Sprouty1 on TCR signaling depending on the differentiation state of the T cell
    • Choi H, Cho SY, Schwartz RH et al (2006) Dual effects of Sprouty1 on TCR signaling depending on the differentiation state of the T cell. J Immunol 176:6034-6045
    • (2006) J Immunol , vol.176 , pp. 6034-6045
    • Choi, H.1    Cho, S.Y.2    Schwartz, R.H.3
  • 31
    • 0034068991 scopus 로고    scopus 로고
    • Differential gene expression by endothelial cells in distinct angiogenic states
    • Glienke J, Schmitt AO, Pilarsky C et al (2000) Differential gene expression by endothelial cells in distinct angiogenic states. Eur J Biochem 267:2820-2830
    • (2000) Eur J Biochem , vol.267 , pp. 2820-2830
    • Glienke, J.1    Schmitt, A.O.2    Pilarsky, C.3
  • 32
    • 0034870220 scopus 로고    scopus 로고
    • Differential gene expression during capillary morphogenesis in 3D collagen matrices: Regulated expression of genes involved in basement membrane matrix assembly, cell cycle progression, cellular differentiation and G-protein signaling
    • Bell SE, Mavila A, Salazar R et al (2001) Differential gene expression during capillary morphogenesis in 3D collagen matrices: regulated expression of genes involved in basement membrane matrix assembly, cell cycle progression, cellular differentiation and G-protein signaling. J Cell Sci 114:2755-2773
    • (2001) J Cell Sci , vol.114 , pp. 2755-2773
    • Bell, S.E.1    Mavila, A.2    Salazar, R.3
  • 33
    • 0035318510 scopus 로고    scopus 로고
    • Tie receptors: New modulators of angiogenic and lymphangiogenic responses
    • Jones N, Iljin K, Dumont DJ et al (2001) Tie receptors: new modulators of angiogenic and lymphangiogenic responses. Nat Rev Mol Cell Biol 2:257-267
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 257-267
    • Jones, N.1    Iljin, K.2    Dumont, D.J.3
  • 34
    • 0141814720 scopus 로고    scopus 로고
    • Endothelial cell diversity revealed by global expression profiling
    • Chi JT, Chang HY, Haraldsen G et al (2003) Endothelial cell diversity revealed by global expression profiling. Proc Natl Acad Sci U S A 100:10623-10628
    • (2003) Proc Natl Acad Sci U S a , vol.100 , pp. 10623-10628
    • Chi, J.T.1    Chang, H.Y.2    Haraldsen, G.3
  • 35
    • 24944461617 scopus 로고    scopus 로고
    • Expression pattern of fibroblast growth factors (FGFs), their receptors and antagonists in primary endothelial cells and vascular smooth muscle cells
    • Antoine M, Wirz W, Tag CG et al (2005) Expression pattern of fibroblast growth factors (FGFs), their receptors and antagonists in primary endothelial cells and vascular smooth muscle cells. Growth Factors 23:87-95
    • (2005) Growth Factors , vol.23 , pp. 87-95
    • Antoine, M.1    Wirz, W.2    Tag, C.G.3
  • 36
    • 33846295218 scopus 로고    scopus 로고
    • FoxOs are lineage-restricted redundant tumor suppressors and regulate endothelial cell homeostasis
    • Paik JH, Kollipara R, Chu G et al (2007) FoxOs are lineage-restricted redundant tumor suppressors and regulate endothelial cell homeostasis. Cell 128:309-323
    • (2007) Cell , vol.128 , pp. 309-323
    • Paik, J.H.1    Kollipara, R.2    Chu, G.3
  • 37
    • 34250214921 scopus 로고    scopus 로고
    • Foxs and Ets in the transcriptional regulation of endothelial cell differentiation and angiogenesis
    • Dejana E, Taddei A, Randi AM (2007) Foxs and Ets in the transcriptional regulation of endothelial cell differentiation and angiogenesis. Biochim Biophys Acta 1775:298-312
    • (2007) Biochim Biophys Acta , vol.1775 , pp. 298-312
    • Dejana, E.1    Taddei, A.2    Randi, A.M.3
  • 38
    • 0344440845 scopus 로고    scopus 로고
    • Functional analysis of the human Sprouty2 gene promoter
    • Ding W, Bellusci S, Shi W et al (2003) Functional analysis of the human Sprouty2 gene promoter. Gene 322:175-185
    • (2003) Gene , vol.322 , pp. 175-185
    • Ding, W.1    Bellusci, S.2    Shi, W.3
  • 39
    • 0035830916 scopus 로고    scopus 로고
    • Inhibition of angiogenesis by a mouse sprouty protein
    • Lee SH, Schloss DJ, Jarvis L et al (2001) Inhibition of angiogenesis by a mouse sprouty protein. J Biol Chem 276:4128-4133
    • (2001) J Biol Chem , vol.276 , pp. 4128-4133
    • Lee, S.H.1    Schloss, D.J.2    Jarvis, L.3
  • 40
    • 0038057388 scopus 로고    scopus 로고
    • Split personalities: The agonistic antagonist Sprouty
    • Christofori G (2003) Split personalities: the agonistic antagonist Sprouty. Nat Cell Biol 5:377-379
    • (2003) Nat Cell Biol , vol.5 , pp. 377-379
    • Christofori, G.1
  • 41
    • 33749438538 scopus 로고    scopus 로고
    • A functional interaction between sprouty proteins and caveolin-1
    • Cabrita MA, Jaggi F, Widjaja SP et al (2006) A functional interaction between sprouty proteins and caveolin-1. J Biol Chem 281:29201-2912
    • (2006) J Biol Chem , vol.281 , pp. 29201-2912
    • Cabrita, M.A.1    Jaggi, F.2    Widjaja, S.P.3
  • 42
    • 33749582985 scopus 로고    scopus 로고
    • A Src homology 3-binding sequence on the C terminus of Sprouty2 is necessary for inhibition of the Ras/ERK pathway downstream of fibroblast growth factor receptor stimulation
    • Lao DH, Chandramouli S, Yusoff P et al (2006) A Src homology 3-binding sequence on the C terminus of Sprouty2 is necessary for inhibition of the Ras/ERK pathway downstream of fibroblast growth factor receptor stimulation. J Biol Chem 281:29993-30000
    • (2006) J Biol Chem , vol.281 , pp. 29993-30000
    • Lao, D.H.1    Chandramouli, S.2    Yusoff, P.3
  • 43
    • 30644457873 scopus 로고    scopus 로고
    • Efficient suppression of FGF-2-induced ERK activation by the cooperative interaction among mammalian Sprouty isoforms
    • Ozaki K, Miyazaki S, Tanimura S et al (2005) Efficient suppression of FGF-2-induced ERK activation by the cooperative interaction among mammalian Sprouty isoforms. J Cell Sci 118:5861-5871
    • (2005) J Cell Sci , vol.118 , pp. 5861-5871
    • Ozaki, K.1    Miyazaki, S.2    Tanimura, S.3
  • 44
    • 0037197922 scopus 로고    scopus 로고
    • The bimodal regulation of epidermal growth factor signaling by human Sprouty proteins
    • Egan JE, Hall AB, Yatsula BA et al (2002) The bimodal regulation of epidermal growth factor signaling by human Sprouty proteins. Proc Natl Acad Sci U S A 99:6041-6046
    • (2002) Proc Natl Acad Sci U S a , vol.99 , pp. 6041-6046
    • Egan, J.E.1    Hall, A.B.2    Yatsula, B.A.3
  • 45
    • 0041856153 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Sprouty2 enhances its interaction with c-Cbl and is crucial for its function
    • Fong CW, Leong HF, Wong ES et al (2003) Tyrosine phosphorylation of Sprouty2 enhances its interaction with c-Cbl and is crucial for its function. J Biol Chem 278:33456-33464
    • (2003) J Biol Chem , vol.278 , pp. 33456-33464
    • Fong, C.W.1    Leong, H.F.2    Wong, E.S.3
  • 46
    • 0242684548 scopus 로고    scopus 로고
    • Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops
    • Rubin C, Litvak V, Medvedovsky H et al (2003) Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops. Curr Biol 13:297-307
    • (2003) Curr Biol , vol.13 , pp. 297-307
    • Rubin, C.1    Litvak, V.2    Medvedovsky, H.3
  • 47
    • 33749332751 scopus 로고    scopus 로고
    • Temporal dynamics of tyrosine phosphorylation in insulin signaling
    • Schmelzle K, Kane S, Gridley S et al (2006) Temporal dynamics of tyrosine phosphorylation in insulin signaling. Diabetes 55:2171-2179
    • (2006) Diabetes , vol.55 , pp. 2171-2179
    • Schmelzle, K.1    Kane, S.2    Gridley, S.3
  • 48
    • 2342453888 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Sprouty proteins regulates their ability to inhibit growth factor signaling: A dual feedback loop
    • Mason JM, Morrison DJ, Bassit B et al (2004) Tyrosine phosphorylation of Sprouty proteins regulates their ability to inhibit growth factor signaling: a dual feedback loop. Mol Biol Cell 15:2176-2188
    • (2004) Mol Biol Cell , vol.15 , pp. 2176-2188
    • Mason, J.M.1    Morrison, D.J.2    Bassit, B.3
  • 49
    • 0036847930 scopus 로고    scopus 로고
    • Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway
    • Hanafusa H, Torii S, Yasunaga T et al (2002) Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway. Nat Cell Biol 4:850-858
    • (2002) Nat Cell Biol , vol.4 , pp. 850-858
    • Hanafusa, H.1    Torii, S.2    Yasunaga, T.3
  • 50
    • 2542433976 scopus 로고    scopus 로고
    • Shp2, an SH2-containing protein-tyrosine phosphatase, positively regulates receptor tyrosine kinase signaling by dephosphorylating and inactivating the inhibitor Sprouty
    • Hanafusa H, Torii S, Yasunaga T et al (2004) Shp2, an SH2-containing protein-tyrosine phosphatase, positively regulates receptor tyrosine kinase signaling by dephosphorylating and inactivating the inhibitor Sprouty. J Biol Chem 279:22992-22995
    • (2004) J Biol Chem , vol.279 , pp. 22992-22995
    • Hanafusa, H.1    Torii, S.2    Yasunaga, T.3
  • 51
    • 33645739909 scopus 로고    scopus 로고
    • Sprouty proteins are in vivo targets of Corkscrew/SHP-2 tyrosine phosphatases
    • Jarvis LA, Toering SJ, Simon MA et al (2006) Sprouty proteins are in vivo targets of Corkscrew/SHP-2 tyrosine phosphatases. Development 133:1133-1142
    • (2006) Development , vol.133 , pp. 1133-1142
    • Jarvis, L.A.1    Toering, S.J.2    Simon, M.A.3
  • 52
    • 12344278405 scopus 로고    scopus 로고
    • FRS2-dependent SRC activation is required for fibroblast growth factor receptor-induced phosphorylation of Sprouty and suppression of ERK activity
    • Li X, Brunton VG, Burgar HR et al (2004) FRS2-dependent SRC activation is required for fibroblast growth factor receptor-induced phosphorylation of Sprouty and suppression of ERK activity. J Cell Sci 117:6007-6017
    • (2004) J Cell Sci , vol.117 , pp. 6007-6017
    • Li, X.1    Brunton, V.G.2    Burgar, H.R.3
  • 53
    • 18144364350 scopus 로고    scopus 로고
    • Fibroblast growth factor/fibroblast growth factor receptor system in angiogenesis
    • Presta M, Dell'Era P, Mitola S et al (2005) Fibroblast growth factor/fibroblast growth factor receptor system in angiogenesis. Cytokine Growth Factor Rev 16:159-178
    • (2005) Cytokine Growth Factor Rev , vol.16 , pp. 159-178
    • Presta, M.1    Dell'Era, P.2    Mitola, S.3
  • 54
    • 0033525895 scopus 로고    scopus 로고
    • Sprouty, an intracellular inhibitor of Ras signaling
    • Casci T, Vinos J, Freeman M (1999) Sprouty, an intracellular inhibitor of Ras signaling. Cell 96:655-665
    • (1999) Cell , vol.96 , pp. 655-665
    • Casci, T.1    Vinos, J.2    Freeman, M.3
  • 55
    • 34548502506 scopus 로고    scopus 로고
    • Sprouty2 binds Grb2 at two different proline-rich regions, and the mechanism of ERK inhibition is independent of this interaction
    • Martinez N, Garcia-Dominguez CA, Domingo B et al (2007) Sprouty2 binds Grb2 at two different proline-rich regions, and the mechanism of ERK inhibition is independent of this interaction. Cell Signal 19:2277-2285
    • (2007) Cell Signal , vol.19 , pp. 2277-2285
    • Martinez, N.1    Garcia-Dominguez, C.A.2    Domingo, B.3
  • 56
    • 15744374069 scopus 로고    scopus 로고
    • Phosphorylation of carboxyl-terminal tyrosines modulates the specificity of Sprouty-2 inhibition of different signaling pathways
    • Rubin C, Zwang Y, Vaisman N et al (2005) Phosphorylation of carboxyl-terminal tyrosines modulates the specificity of Sprouty-2 inhibition of different signaling pathways. J Biol Chem 280:9735-9744
    • (2005) J Biol Chem , vol.280 , pp. 9735-9744
    • Rubin, C.1    Zwang, Y.2    Vaisman, N.3
  • 57
    • 34247866596 scopus 로고    scopus 로고
    • Direct binding of PP2A to Sprouty2 and phosphorylation changes are a prerequisite for ERK inhibition downstream of fibroblast growth factor receptor stimulation
    • Lao DH, Yusoff P, Chandramouli S et al (2007) Direct binding of PP2A to Sprouty2 and phosphorylation changes are a prerequisite for ERK inhibition downstream of fibroblast growth factor receptor stimulation. J Biol Chem 282:9117-9126
    • (2007) J Biol Chem , vol.282 , pp. 9117-9126
    • Lao, D.H.1    Yusoff, P.2    Chandramouli, S.3
  • 58
    • 33644546368 scopus 로고    scopus 로고
    • Tumor endothelial cells express epidermal growth factor receptor (EGFR) but not ErbB3 and are responsive to EGF and to EGFR kinase inhibitors
    • Amin DN, Hida K, Bielenberg DR et al (2006) Tumor endothelial cells express epidermal growth factor receptor (EGFR) but not ErbB3 and are responsive to EGF and to EGFR kinase inhibitors. Cancer Res 66:2173-2180
    • (2006) Cancer Res , vol.66 , pp. 2173-2180
    • Amin, D.N.1    Hida, K.2    Bielenberg, D.R.3
  • 59
    • 20444431504 scopus 로고    scopus 로고
    • The antitumor and antiangiogenic activity of vascular endothelial growth factor receptor inhibition is potentiated by ErbB1 blockade
    • Sini P, Wyder L, Schnell C et al (2005) The antitumor and antiangiogenic activity of vascular endothelial growth factor receptor inhibition is potentiated by ErbB1 blockade. Clin Cancer Res 11:4521-4532
    • (2005) Clin Cancer Res , vol.11 , pp. 4521-4532
    • Sini, P.1    Wyder, L.2    Schnell, C.3
  • 60
    • 28044433677 scopus 로고    scopus 로고
    • Epidermal growth factor receptor and angiogenesis: Opportunities for combined anticancer strategies
    • van Cruijsen H, Giaccone G, Hoekman K (2005) Epidermal growth factor receptor and angiogenesis: Opportunities for combined anticancer strategies. Int J Cancer 117:883-888
    • (2005) Int J Cancer , vol.117 , pp. 883-888
    • Van Cruijsen, H.1    Giaccone, G.2    Hoekman, K.3
  • 61
    • 0037119950 scopus 로고    scopus 로고
    • Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling
    • Wong ES, Fong CW, Lim J et al (2002) Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling. EMBO J 21:4796-4808
    • (2002) EMBO J , vol.21 , pp. 4796-4808
    • Wong, E.S.1    Fong, C.W.2    Lim, J.3
  • 62
    • 0035937167 scopus 로고    scopus 로고
    • Evidence for direct interaction between Sprouty and Cbl
    • Wong ES, Lim J, Low BC et al (2001) Evidence for direct interaction between Sprouty and Cbl. J Biol Chem 276:5866-5875
    • (2001) J Biol Chem , vol.276 , pp. 5866-5875
    • Wong, E.S.1    Lim, J.2    Low, B.C.3
  • 63
    • 23744489852 scopus 로고    scopus 로고
    • Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation
    • Haglund K, Schmidt MH, Wong ES et al (2005) Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation. EMBO Rep 6:635-641
    • (2005) EMBO Rep , vol.6 , pp. 635-641
    • Haglund, K.1    Schmidt, M.H.2    Wong, E.S.3
  • 64
    • 33847260172 scopus 로고    scopus 로고
    • Spatial regulation of EGFR signaling by Sprouty2
    • Kim HJ, Taylor LJ, Bar-Sagi D (2007) Spatial regulation of EGFR signaling by Sprouty2. Curr Biol 17:455-461
    • (2007) Curr Biol , vol.17 , pp. 455-461
    • Kim, H.J.1    Taylor, L.J.2    Bar-Sagi, D.3
  • 65
    • 30744432619 scopus 로고    scopus 로고
    • Endothelial cells and VEGF in vascular development
    • Coultas L, Chawengsaksophak K, Rossant J (2005) Endothelial cells and VEGF in vascular development. Nature 438:937-945
    • (2005) Nature , vol.438 , pp. 937-945
    • Coultas, L.1    Chawengsaksophak, K.2    Rossant, J.3
  • 66
    • 0035355472 scopus 로고    scopus 로고
    • A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells
    • Takahashi T, Yamaguchi S, Chida K et al (2001) A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells. EMBO J 20:2768-2778
    • (2001) EMBO J , vol.20 , pp. 2768-2778
    • Takahashi, T.1    Yamaguchi, S.2    Chida, K.3
  • 67
    • 0038613087 scopus 로고    scopus 로고
    • Mammalian Sprouty4 suppresses Ras-independent ERK activation by binding to Raf1
    • Sasaki A, Taketomi T, Kato R et al (2003) Mammalian Sprouty4 suppresses Ras-independent ERK activation by binding to Raf1. Nat Cell Biol 5:427-432
    • (2003) Nat Cell Biol , vol.5 , pp. 427-432
    • Sasaki, A.1    Taketomi, T.2    Kato, R.3
  • 69
    • 19944428563 scopus 로고    scopus 로고
    • Endothelial-specific expression of caveolin-1 impairs microvascular permeability and angiogenesis
    • Bauer PM, Yu J, Chen Y et al (2005) Endothelial-specific expression of caveolin-1 impairs microvascular permeability and angiogenesis. Proc Natl Acad Sci U S A 102:204-209
    • (2005) Proc Natl Acad Sci U S a , vol.102 , pp. 204-209
    • Bauer, P.M.1    Yu, J.2    Chen, Y.3
  • 70
    • 34047251876 scopus 로고    scopus 로고
    • Caveolin-1-deficient mice have increased tumor microvascular permeability, angiogenesis, and growth
    • Lin MI, Yu J, Murata T et al (2007) Caveolin-1-deficient mice have increased tumor microvascular permeability, angiogenesis, and growth. Cancer Res 67:2849-2856
    • (2007) Cancer Res , vol.67 , pp. 2849-2856
    • Lin, M.I.1    Yu, J.2    Murata, T.3
  • 71
    • 0037155864 scopus 로고    scopus 로고
    • Caveolin-1 expression enhances endothelial capillary tubule formation
    • Liu J, Wang XB, Park DS et al (2002) Caveolin-1 expression enhances endothelial capillary tubule formation. J Biol Chem 277:10661-10668
    • (2002) J Biol Chem , vol.277 , pp. 10661-10668
    • Liu, J.1    Wang, X.B.2    Park, D.S.3
  • 72
    • 0038075402 scopus 로고    scopus 로고
    • Caveolin-1 knockout mice show an impaired angiogenic response to exogenous stimuli
    • Woodman SE, Ashton AW, Schubert W et al (2003) Caveolin-1 knockout mice show an impaired angiogenic response to exogenous stimuli. Am J Pathol 162:2059-2068
    • (2003) Am J Pathol , vol.162 , pp. 2059-2068
    • Woodman, S.E.1    Ashton, A.W.2    Schubert, W.3
  • 73
    • 0032538790 scopus 로고    scopus 로고
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade
    • Galbiati F, Volonte D, Engelman JA et al (1998) Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade. EMBO J 17:6633-6648
    • (1998) EMBO J , vol.17 , pp. 6633-6648
    • Galbiati, F.1    Volonte, D.2    Engelman, J.A.3
  • 74
    • 33847612502 scopus 로고    scopus 로고
    • Regulation of platelet-derived growth factor-induced Ras signaling by poliovirus receptor Necl-5 and negative growth regulator Sprouty2
    • Kajita M, Ikeda W, Tamaru Y et al (2007) Regulation of platelet-derived growth factor-induced Ras signaling by poliovirus receptor Necl-5 and negative growth regulator Sprouty2. Genes Cells 12:345-357
    • (2007) Genes Cells , vol.12 , pp. 345-357
    • Kajita, M.1    Ikeda, W.2    Tamaru, Y.3
  • 75
    • 35548989353 scopus 로고    scopus 로고
    • The roles of nectins in cell adhesions: Cooperation with other cell adhesion molecules and growth factor receptors
    • Sakisaka T, Ikeda W, Ogita H et al (2007) The roles of nectins in cell adhesions: cooperation with other cell adhesion molecules and growth factor receptors. Curr Opin Cell Biol 19:593-602
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 593-602
    • Sakisaka, T.1    Ikeda, W.2    Ogita, H.3
  • 76
    • 0025141614 scopus 로고
    • Poliovirus permissivity and specific receptor expression on human endothelial cells
    • Couderc T, Barzu T, Horaud F et al (1990) Poliovirus permissivity and specific receptor expression on human endothelial cells. Virology 174:95-102
    • (1990) Virology , vol.174 , pp. 95-102
    • Couderc, T.1    Barzu, T.2    Horaud, F.3
  • 77
    • 38349087514 scopus 로고    scopus 로고
    • Tesk1 interacts with sprouty2 to abrogate its inhibition of ERK phosphorylation downstream of receptor tyrosine kinase signaling
    • Chandramouli S, Yu CY, Yusoff P et al (2008) Tesk1 interacts with sprouty2 to abrogate its inhibition of ERK phosphorylation downstream of receptor tyrosine kinase signaling. J Biol Chem 283:1679-1691
    • (2008) J Biol Chem , vol.283 , pp. 1679-1691
    • Chandramouli, S.1    Yu, C.Y.2    Yusoff, P.3
  • 78
    • 18844451747 scopus 로고    scopus 로고
    • Sprouty-4 negatively regulates cell spreading by inhibiting the kinase activity of testicular protein kinase
    • Tsumura Y, Toshima J, Leeksma OC et al (2005) Sprouty-4 negatively regulates cell spreading by inhibiting the kinase activity of testicular protein kinase. Biochem J 387:627-637
    • (2005) Biochem J , vol.387 , pp. 627-637
    • Tsumura, Y.1    Toshima, J.2    Leeksma, O.C.3
  • 79
    • 0034801558 scopus 로고    scopus 로고
    • ERK pathway positively regulates the expression of Sprouty genes
    • Ozaki K, Kadomoto R, Asato K et al (2001) ERK pathway positively regulates the expression of Sprouty genes. Biochem Biophys Res Commun 285:1084-1088
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 1084-1088
    • Ozaki, K.1    Kadomoto, R.2    Asato, K.3
  • 80
    • 0037452567 scopus 로고    scopus 로고
    • HSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl
    • Hall AB, Jura N, DaSilva J et al (2003) hSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl. Curr Biol 13:308-314
    • (2003) Curr Biol , vol.13 , pp. 308-314
    • Hall, A.B.1    Jura, N.2    Dasilva, J.3
  • 81
    • 19644367829 scopus 로고    scopus 로고
    • Negative regulation of receptor tyrosine kinases: Unexpected links to c-Cbl and receptor ubiquitylation
    • Rubin C, Gur G, Yarden Y (2005) Negative regulation of receptor tyrosine kinases: unexpected links to c-Cbl and receptor ubiquitylation. Cell Res 15:66-71
    • (2005) Cell Res , vol.15 , pp. 66-71
    • Rubin, C.1    Gur, G.2    Yarden, Y.3
  • 82
    • 33644521566 scopus 로고    scopus 로고
    • Regulation of sprouty stability by Mnk1-dependent phosphorylation
    • DaSilva J, Xu L, Kim HJ et al (2006) Regulation of sprouty stability by Mnk1-dependent phosphorylation. Mol Cell Biol 26:1898-1907
    • (2006) Mol Cell Biol , vol.26 , pp. 1898-1907
    • Dasilva, J.1    Xu, L.2    Kim, H.J.3
  • 83
    • 34547939708 scopus 로고    scopus 로고
    • Sprouty2 downregulation plays a pivotal role in mediating crosstalk between TGF-beta1 signaling and EGF as well as FGF receptor tyrosine kinase-ERK pathways in mesenchymal cells
    • Ding W, Shi W, Bellusci S et al (2007) Sprouty2 downregulation plays a pivotal role in mediating crosstalk between TGF-beta1 signaling and EGF as well as FGF receptor tyrosine kinase-ERK pathways in mesenchymal cells. J Cell Physiol 212:796-806
    • (2007) J Cell Physiol , vol.212 , pp. 796-806
    • Ding, W.1    Shi, W.2    Bellusci, S.3
  • 84
    • 33845673574 scopus 로고    scopus 로고
    • Regulation of Sprouty2 stability by mammalian Seven-in-Absentia homolog 2
    • Nadeau RJ, Toher JL, Yang X et al (2007) Regulation of Sprouty2 stability by mammalian Seven-in-Absentia homolog 2. J Cell Biochem 100:151-160
    • (2007) J Cell Biochem , vol.100 , pp. 151-160
    • Nadeau, R.J.1    Toher, J.L.2    Yang, X.3
  • 85
    • 0038376002 scopus 로고    scopus 로고
    • Molecular regulation of vessel maturation
    • Jain RK (2003) Molecular regulation of vessel maturation. Nat Med 9:685-693
    • (2003) Nat Med , vol.9 , pp. 685-693
    • Jain, R.K.1
  • 86
    • 25444484692 scopus 로고    scopus 로고
    • Mammalian sprouty proteins assemble into large monodisperse particles having the properties of intracellular nanobatteries
    • Wu X, Alexander PB, He Y et al (2005) Mammalian sprouty proteins assemble into large monodisperse particles having the properties of intracellular nanobatteries. Proc Natl Acad Sci U S A 102:14058-14062
    • (2005) Proc Natl Acad Sci U S a , vol.102 , pp. 14058-14062
    • Wu, X.1    Alexander, P.B.2    He, Y.3
  • 87
    • 0033538439 scopus 로고    scopus 로고
    • Nitric oxide contributes to behavioral, cellular, and developmental responses to low oxygen in Drosophila
    • Wingrove JA, O'Farrell PH (1999) Nitric oxide contributes to behavioral, cellular, and developmental responses to low oxygen in Drosophila. Cell 98:105-114
    • (1999) Cell , vol.98 , pp. 105-114
    • Wingrove, J.A.1    O'Farrell, P.H.2
  • 88
    • 33847711009 scopus 로고    scopus 로고
    • An emerging role for endothelial nitric oxide synthase in chronic inflammation and cancer
    • Ying L, Hofseth LJ (2007) An emerging role for endothelial nitric oxide synthase in chronic inflammation and cancer. Cancer Res 67:1407-1410
    • (2007) Cancer Res , vol.67 , pp. 1407-1410
    • Ying, L.1    Hofseth, L.J.2
  • 90
    • 33751015460 scopus 로고    scopus 로고
    • Branching morphogenesis of the ureteric epithelium during kidney development is coordinated by the opposing functions of GDNF and Sprouty1
    • Basson MA, Watson-Johnson J, Shakya R et al (2006) Branching morphogenesis of the ureteric epithelium during kidney development is coordinated by the opposing functions of GDNF and Sprouty1. Dev Biol 299:466-477
    • (2006) Dev Biol , vol.299 , pp. 466-477
    • Basson, M.A.1    Watson-Johnson, J.2    Shakya, R.3
  • 91
    • 16244423015 scopus 로고    scopus 로고
    • Sprouty2, a mouse deafness gene, regulates cell fate decisions in the auditory sensory epithelium by antagonizing FGF signaling
    • Shim K, Minowada G, Coling DE et al (2005) Sprouty2, a mouse deafness gene, regulates cell fate decisions in the auditory sensory epithelium by antagonizing FGF signaling. Dev Cell 8:553-564
    • (2005) Dev Cell , vol.8 , pp. 553-564
    • Shim, K.1    Minowada, G.2    Coling, D.E.3
  • 92
    • 24944448766 scopus 로고    scopus 로고
    • Loss of mammalian Sprouty2 leads to enteric neuronal hyperplasia and esophageal achalasia
    • Taketomi T, Yoshiga D, Taniguchi K et al (2005) Loss of mammalian Sprouty2 leads to enteric neuronal hyperplasia and esophageal achalasia. Nat Neurosci 8:855-857
    • (2005) Nat Neurosci , vol.8 , pp. 855-857
    • Taketomi, T.1    Yoshiga, D.2    Taniguchi, K.3
  • 93
    • 33746696103 scopus 로고    scopus 로고
    • Sprouty genes control diastema tooth development via bidirectional antagonism of epithelial-mesenchymal FGF signaling
    • Klein OD, Minowada G, Peterkova R et al (2006) Sprouty genes control diastema tooth development via bidirectional antagonism of epithelial- mesenchymal FGF signaling. Dev Cell 11:181-190
    • (2006) Dev Cell , vol.11 , pp. 181-190
    • Klein, O.D.1    Minowada, G.2    Peterkova, R.3
  • 94
    • 33845412960 scopus 로고    scopus 로고
    • Sprouty2 and Sprouty4 are essential for embryonic morphogenesis and regulation of FGF signaling
    • Taniguchi K, Ayada T, Ichiyama K et al (2007) Sprouty2 and Sprouty4 are essential for embryonic morphogenesis and regulation of FGF signaling. Biochem Biophys Res Commun 352:896-902
    • (2007) Biochem Biophys Res Commun , vol.352 , pp. 896-902
    • Taniguchi, K.1    Ayada, T.2    Ichiyama, K.3
  • 95
    • 17844381597 scopus 로고    scopus 로고
    • FGF signal interpretation is directed by Sprouty and Spred proteins during mesoderm formation
    • 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
    • (2005) Dev Cell , vol.8 , pp. 689-701
    • Sivak, J.M.1    Petersen, L.F.2    Amaya, E.3
  • 96
    • 34250165403 scopus 로고    scopus 로고
    • Spreds are essential for embryonic lymphangiogenesis by regulating vascular endothelial growth factor receptor 3 signaling
    • Taniguchi K, Kohno R, Ayada T et al (2007) Spreds are essential for embryonic lymphangiogenesis by regulating vascular endothelial growth factor receptor 3 signaling. Mol Cell Biol 27:4541-4550
    • (2007) Mol Cell Biol , vol.27 , pp. 4541-4550
    • Taniguchi, K.1    Kohno, R.2    Ayada, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.