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Volumn 1813, Issue 2, 2011, Pages 332-339

The type III TGF-β receptor betaglycan transmembrane-cytoplasmic domain fragment is stable after ectodomain cleavage and is a substrate of the intramembrane protease β-secretase

Author keywords

Secretase; Betaglycan; Ectodomain shedding; Regulated intramembrane proteolysis; TGF

Indexed keywords

GAMMA SECRETASE; PROTEOGLYCAN; SERINE; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 3;

EID: 78650964786     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.12.005     Document Type: Article
Times cited : (19)

References (77)
  • 1
    • 0026672711 scopus 로고
    • Binding of two growth factor families to separate domains of the proteoglycan betaglycan
    • Andres J.L., DeFalcis D., Noda M., Massague J. Binding of two growth factor families to separate domains of the proteoglycan betaglycan. J. Biol. Chem. 1992, 267:5927-5930.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5927-5930
    • Andres, J.L.1    DeFalcis, D.2    Noda, M.3    Massague, J.4
  • 2
    • 0028291369 scopus 로고
    • The types II and III transforming growth factor-beta receptors form homo-oligomers
    • Henis Y.I., Moustakas A., Lin H.Y., Lodish H.F. The types II and III transforming growth factor-beta receptors form homo-oligomers. J. Cell Biol. 1994, 126:139-154.
    • (1994) J. Cell Biol. , vol.126 , pp. 139-154
    • Henis, Y.I.1    Moustakas, A.2    Lin, H.Y.3    Lodish, H.F.4
  • 3
    • 0025987832 scopus 로고
    • Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system
    • Lopez-Casillas F., Cheifetz S., Doody J., Andres J.L., Lane W.S., Massague J. Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system. Cell 1991, 67:785-795.
    • (1991) Cell , vol.67 , pp. 785-795
    • Lopez-Casillas, F.1    Cheifetz, S.2    Doody, J.3    Andres, J.L.4    Lane, W.S.5    Massague, J.6
  • 4
    • 0027276765 scopus 로고
    • Betaglycan presents ligand to the TGF beta signaling receptor
    • Lopez-Casillas F., Wrana J.L., Massague J. Betaglycan presents ligand to the TGF beta signaling receptor. Cell 1993, 73:1435-1444.
    • (1993) Cell , vol.73 , pp. 1435-1444
    • Lopez-Casillas, F.1    Wrana, J.L.2    Massague, J.3
  • 5
    • 0027490673 scopus 로고
    • The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand
    • Moustakas A., Lin H.Y., Henis Y.I., Plamondon J., O'Connor-McCourt M.D., Lodish H.F. The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand. J. Biol. Chem. 1993, 268:22215-22218.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22215-22218
    • Moustakas, A.1    Lin, H.Y.2    Henis, Y.I.3    Plamondon, J.4    O'Connor-McCourt, M.D.5    Lodish, H.F.6
  • 6
  • 7
    • 0033605704 scopus 로고    scopus 로고
    • Requirement of type III TGF-beta receptor for endocardial cell transformation in the heart
    • Brown C.B., Boyer A.S., Runyan R.B., Barnett J.V. Requirement of type III TGF-beta receptor for endocardial cell transformation in the heart. Science 1999, 283:2080-2082.
    • (1999) Science , vol.283 , pp. 2080-2082
    • Brown, C.B.1    Boyer, A.S.2    Runyan, R.B.3    Barnett, J.V.4
  • 8
    • 35448946457 scopus 로고    scopus 로고
    • Coronary vessel development is dependent on the type III transforming growth factor beta receptor
    • Compton L.A., Potash D.A., Brown C.B., Barnett J.V. Coronary vessel development is dependent on the type III transforming growth factor beta receptor. Circ. Res. 2007, 101:784-791.
    • (2007) Circ. Res. , vol.101 , pp. 784-791
    • Compton, L.A.1    Potash, D.A.2    Brown, C.B.3    Barnett, J.V.4
  • 9
    • 33747015300 scopus 로고    scopus 로고
    • Extracellular proteoglycans modify TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation
    • Droguett R., Cabello-Verrugio C., Riquelme C., Brandan E. Extracellular proteoglycans modify TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation. Matrix Biol. 2006, 25:332-341.
    • (2006) Matrix Biol. , vol.25 , pp. 332-341
    • Droguett, R.1    Cabello-Verrugio, C.2    Riquelme, C.3    Brandan, E.4
  • 11
  • 14
    • 40949157944 scopus 로고    scopus 로고
    • TbetaRIII suppresses non-small cell lung cancer invasiveness and tumorigenicity
    • Finger E.C., Turley R.S., Dong M., How T., Fields T.A., Blobe G.C. TbetaRIII suppresses non-small cell lung cancer invasiveness and tumorigenicity. Carcinogenesis 2008, 29:528-535.
    • (2008) Carcinogenesis , vol.29 , pp. 528-535
    • Finger, E.C.1    Turley, R.S.2    Dong, M.3    How, T.4    Fields, T.A.5    Blobe, G.C.6
  • 15
    • 34347226354 scopus 로고    scopus 로고
    • Loss of betaglycan expression in ovarian cancer: role in motility and invasion
    • Hempel N., How T., Dong M., Murphy S.K., Fields T.A., Blobe G.C. Loss of betaglycan expression in ovarian cancer: role in motility and invasion. Cancer Res. 2007, 67:5231-5238.
    • (2007) Cancer Res. , vol.67 , pp. 5231-5238
    • Hempel, N.1    How, T.2    Dong, M.3    Murphy, S.K.4    Fields, T.A.5    Blobe, G.C.6
  • 16
    • 33751178827 scopus 로고    scopus 로고
    • Stem cells in prostate cancer: resolving the castrate-resistant conundrum and implications for hormonal therapy
    • Sharifi N., Kawasaki B.T., Hurt E.M., Farrar W.L. Stem cells in prostate cancer: resolving the castrate-resistant conundrum and implications for hormonal therapy. Cancer Biol. Ther. 2006, 5:901-906.
    • (2006) Cancer Biol. Ther. , vol.5 , pp. 901-906
    • Sharifi, N.1    Kawasaki, B.T.2    Hurt, E.M.3    Farrar, W.L.4
  • 17
    • 33847069683 scopus 로고    scopus 로고
    • The type III transforming growth factor-beta receptor as a novel tumor suppressor gene in prostate cancer
    • Turley R.S., Finger E.C., Hempel N., How T., Fields T.A., Blobe G.C. The type III transforming growth factor-beta receptor as a novel tumor suppressor gene in prostate cancer. Cancer Res. 2007, 67:1090-1098.
    • (2007) Cancer Res. , vol.67 , pp. 1090-1098
    • Turley, R.S.1    Finger, E.C.2    Hempel, N.3    How, T.4    Fields, T.A.5    Blobe, G.C.6
  • 18
    • 54749147136 scopus 로고    scopus 로고
    • Knockdown of the transforming growth factor-beta type III receptor impairs motility and invasion of metastatic cancer cells
    • Criswell T.L., Dumont N., Barnett J.V., Arteaga C.L. Knockdown of the transforming growth factor-beta type III receptor impairs motility and invasion of metastatic cancer cells. Cancer Res. 2008, 68:7304-7312.
    • (2008) Cancer Res. , vol.68 , pp. 7304-7312
    • Criswell, T.L.1    Dumont, N.2    Barnett, J.V.3    Arteaga, C.L.4
  • 19
    • 33744784611 scopus 로고    scopus 로고
    • Betaglycan induces TGF-beta signaling in a ligand-independent manner, through activation of the p38 pathway
    • Santander C., Brandan E. Betaglycan induces TGF-beta signaling in a ligand-independent manner, through activation of the p38 pathway. Cell. Signal. 2006, 18:1482-1491.
    • (2006) Cell. Signal. , vol.18 , pp. 1482-1491
    • Santander, C.1    Brandan, E.2
  • 20
    • 36949015426 scopus 로고    scopus 로고
    • The type III TGF-beta receptor signals through both Smad3 and the p38 MAP kinase pathways to contribute to inhibition of cell proliferation
    • You H.J., Bruinsma M.W., How T., Ostrander J.H., Blobe G.C. The type III TGF-beta receptor signals through both Smad3 and the p38 MAP kinase pathways to contribute to inhibition of cell proliferation. Carcinogenesis 2007, 28:2491-2500.
    • (2007) Carcinogenesis , vol.28 , pp. 2491-2500
    • You, H.J.1    Bruinsma, M.W.2    How, T.3    Ostrander, J.H.4    Blobe, G.C.5
  • 21
    • 0029871789 scopus 로고    scopus 로고
    • Betaglycan has multiple binding sites for transforming growth factor-beta 1
    • Kaname S., Ruoslahti E. Betaglycan has multiple binding sites for transforming growth factor-beta 1. Biochem. J. 1996, 315(Pt 3):815-820.
    • (1996) Biochem. J. , vol.315 , Issue.PT 3 , pp. 815-820
    • Kaname, S.1    Ruoslahti, E.2
  • 22
    • 0029066003 scopus 로고
    • Expression of transforming growth factor type III receptor in vascular endothelial cells increases their responsiveness to transforming growth factor beta 2
    • Sankar S., Mahooti-Brooks N., Centrella M., McCarthy T.L., Madri J.A. Expression of transforming growth factor type III receptor in vascular endothelial cells increases their responsiveness to transforming growth factor beta 2. J. Biol. Chem. 1995, 270:13567-13572.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13567-13572
    • Sankar, S.1    Mahooti-Brooks, N.2    Centrella, M.3    McCarthy, T.L.4    Madri, J.A.5
  • 23
    • 2542425404 scopus 로고    scopus 로고
    • In the absence of type III receptor, the transforming growth factor (TGF)-beta type II-B receptor requires the type I receptor to bind TGF-beta2
    • del Re E., Babitt J.L., Pirani A., Schneyer A.L., Lin H.Y. In the absence of type III receptor, the transforming growth factor (TGF)-beta type II-B receptor requires the type I receptor to bind TGF-beta2. J. Biol. Chem. 2004, 279:22765-22772.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22765-22772
    • del Re, E.1    Babitt, J.L.2    Pirani, A.3    Schneyer, A.L.4    Lin, H.Y.5
  • 24
    • 0028999341 scopus 로고
    • Cooperative binding of transforming growth factor (TGF)-beta 2 to the types I and II TGF-beta receptors
    • Rodriguez C., Chen F., Weinberg R.A., Lodish H.F. Cooperative binding of transforming growth factor (TGF)-beta 2 to the types I and II TGF-beta receptors. J. Biol. Chem. 1995, 270:15919-15922.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15919-15922
    • Rodriguez, C.1    Chen, F.2    Weinberg, R.A.3    Lodish, H.F.4
  • 25
    • 0035254335 scopus 로고    scopus 로고
    • Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor
    • Rotzer D., Roth M., Lutz M., Lindemann D., Sebald W., Knaus P. Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor. EMBO J. 2001, 20:480-490.
    • (2001) EMBO J. , vol.20 , pp. 480-490
    • Rotzer, D.1    Roth, M.2    Lutz, M.3    Lindemann, D.4    Sebald, W.5    Knaus, P.6
  • 26
    • 0037206410 scopus 로고    scopus 로고
    • Properties of inhibin binding to betaglycan, InhBP/p120 and the activin type II receptors
    • Chapman S.C., Bernard D.J., Jelen J., Woodruff T.K. Properties of inhibin binding to betaglycan, InhBP/p120 and the activin type II receptors. Mol. Cell. Endocrinol. 2002, 196:79-93.
    • (2002) Mol. Cell. Endocrinol. , vol.196 , pp. 79-93
    • Chapman, S.C.1    Bernard, D.J.2    Jelen, J.3    Woodruff, T.K.4
  • 27
    • 0035805505 scopus 로고    scopus 로고
    • Ligand binding and functional properties of betaglycan, a co-receptor of the transforming growth factor-beta superfamily. Specialized binding regions for transforming growth factor-beta and inhibin A
    • Esparza-Lopez J., Montiel J.L., Vilchis-Landeros M.M., Okadome T., Miyazono K., Lopez-Casillas F. Ligand binding and functional properties of betaglycan, a co-receptor of the transforming growth factor-beta superfamily. Specialized binding regions for transforming growth factor-beta and inhibin A. J. Biol. Chem. 2001, 276:14588-14596.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14588-14596
    • Esparza-Lopez, J.1    Montiel, J.L.2    Vilchis-Landeros, M.M.3    Okadome, T.4    Miyazono, K.5    Lopez-Casillas, F.6
  • 28
    • 43149095145 scopus 로고    scopus 로고
    • Bone morphogenetic proteins signal through the transforming growth factor-beta type III receptor
    • Kirkbride K.C., Townsend T.A., Bruinsma M.W., Barnett J.V., Blobe G.C. Bone morphogenetic proteins signal through the transforming growth factor-beta type III receptor. J. Biol. Chem. 2008, 283:7628-7637.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7628-7637
    • Kirkbride, K.C.1    Townsend, T.A.2    Bruinsma, M.W.3    Barnett, J.V.4    Blobe, G.C.5
  • 30
    • 47749090950 scopus 로고    scopus 로고
    • Suppression of inhibin A biological activity by alterations in the binding site for betaglycan
    • Makanji Y., Walton K.L., Wilce M.C., Chan K.L., Robertson D.M., Harrison C.A. Suppression of inhibin A biological activity by alterations in the binding site for betaglycan. J. Biol. Chem. 2008, 283:16743-16751.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16743-16751
    • Makanji, Y.1    Walton, K.L.2    Wilce, M.C.3    Chan, K.L.4    Robertson, D.M.5    Harrison, C.A.6
  • 31
    • 33745124059 scopus 로고    scopus 로고
    • Inhibins differentially antagonize activin and bone morphogenetic protein action in a mouse adrenocortical cell line
    • Farnworth P.G., Stanton P.G., Wang Y., Escalona R., Findlay J.K., Ooi G.T. Inhibins differentially antagonize activin and bone morphogenetic protein action in a mouse adrenocortical cell line. Endocrinology 2006, 147:3462-3471.
    • (2006) Endocrinology , vol.147 , pp. 3462-3471
    • Farnworth, P.G.1    Stanton, P.G.2    Wang, Y.3    Escalona, R.4    Findlay, J.K.5    Ooi, G.T.6
  • 32
    • 0037016690 scopus 로고    scopus 로고
    • Betaglycan inhibits TGF-beta signaling by preventing type I-type II receptor complex formation. Glycosaminoglycan modifications alter betaglycan function
    • Eickelberg O., Centrella M., Reiss M., Kashgarian M., Wells R.G. Betaglycan inhibits TGF-beta signaling by preventing type I-type II receptor complex formation. Glycosaminoglycan modifications alter betaglycan function. J. Biol. Chem. 2002, 277:823-829.
    • (2002) J. Biol. Chem. , vol.277 , pp. 823-829
    • Eickelberg, O.1    Centrella, M.2    Reiss, M.3    Kashgarian, M.4    Wells, R.G.5
  • 33
    • 0037424231 scopus 로고    scopus 로고
    • Inhibin is an antagonist of bone morphogenetic protein signaling
    • Wiater E., Vale W. Inhibin is an antagonist of bone morphogenetic protein signaling. J. Biol. Chem. 2003, 278:7934-7941.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7934-7941
    • Wiater, E.1    Vale, W.2
  • 34
    • 0024792629 scopus 로고
    • Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta
    • Andres J.L., Stanley K., Cheifetz S., Massague J. Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta. J. Cell Biol. 1989, 109:3137-3145.
    • (1989) J. Cell Biol. , vol.109 , pp. 3137-3145
    • Andres, J.L.1    Stanley, K.2    Cheifetz, S.3    Massague, J.4
  • 35
    • 0033135695 scopus 로고    scopus 로고
    • Ectodomain cleavage and shedding of the type III transforming growth factor-beta receptor in lung membranes effect of temperature, ligand binding and membrane solubilization
    • Philip A., Hannah R., O'Connor-McCourt M. Ectodomain cleavage and shedding of the type III transforming growth factor-beta receptor in lung membranes effect of temperature, ligand binding and membrane solubilization. Eur. J. Biochem. 1999, 261:618-628.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 618-628
    • Philip, A.1    Hannah, R.2    O'Connor-McCourt, M.3
  • 36
    • 1542289879 scopus 로고    scopus 로고
    • The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1
    • Velasco-Loyden G., Arribas J., Lopez-Casillas F. The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1. J. Biol. Chem. 2004, 279:7721-7733.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7721-7733
    • Velasco-Loyden, G.1    Arribas, J.2    Lopez-Casillas, F.3
  • 38
    • 14944363173 scopus 로고    scopus 로고
    • Systemic administration of a soluble betaglycan suppresses tumor growth, angiogenesis, and matrix metalloproteinase-9 expression in a human xenograft model of prostate cancer
    • Bandyopadhyay A., Wang L., Lopez-Casillas F., Mendoza V., Yeh I.T., Sun L. Systemic administration of a soluble betaglycan suppresses tumor growth, angiogenesis, and matrix metalloproteinase-9 expression in a human xenograft model of prostate cancer. Prostate 2005, 63:81-90.
    • (2005) Prostate , vol.63 , pp. 81-90
    • Bandyopadhyay, A.1    Wang, L.2    Lopez-Casillas, F.3    Mendoza, V.4    Yeh, I.T.5    Sun, L.6
  • 41
    • 0036468719 scopus 로고    scopus 로고
    • Soluble transforming growth factor-beta type III receptor gene transfection inhibits fibrous airway obliteration in a rat model of Bronchiolitis obliterans
    • Liu M., Suga M., Maclean A.A., St George J.A., Souza D.W., Keshavjee S. Soluble transforming growth factor-beta type III receptor gene transfection inhibits fibrous airway obliteration in a rat model of Bronchiolitis obliterans. Am. J. Respir. Crit. Care Med. 2002, 165:419-423.
    • (2002) Am. J. Respir. Crit. Care Med. , vol.165 , pp. 419-423
    • Liu, M.1    Suga, M.2    Maclean, A.A.3    St George, J.A.4    Souza, D.W.5    Keshavjee, S.6
  • 42
    • 54049145076 scopus 로고    scopus 로고
    • Glioma gene therapy with soluble transforming growth factor-beta receptors II and III
    • Naumann U., Maass P., Gleske A.K., Aulwurm S., Weller M., Eisele G. Glioma gene therapy with soluble transforming growth factor-beta receptors II and III. Int. J. Oncol. 2008, 33:759-765.
    • (2008) Int. J. Oncol. , vol.33 , pp. 759-765
    • Naumann, U.1    Maass, P.2    Gleske, A.K.3    Aulwurm, S.4    Weller, M.5    Eisele, G.6
  • 43
    • 0035310360 scopus 로고    scopus 로고
    • Recombinant soluble betaglycan is a potent and isoform-selective transforming growth factor-beta neutralizing agent
    • Vilchis-Landeros M.M., Montiel J.L., Mendoza V., Mendoza-Hernandez G., Lopez-Casillas F. Recombinant soluble betaglycan is a potent and isoform-selective transforming growth factor-beta neutralizing agent. Biochem. J. 2001, 355:215-222.
    • (2001) Biochem. J. , vol.355 , pp. 215-222
    • Vilchis-Landeros, M.M.1    Montiel, J.L.2    Mendoza, V.3    Mendoza-Hernandez, G.4    Lopez-Casillas, F.5
  • 44
    • 71549129301 scopus 로고    scopus 로고
    • Betaglycan has two independent domains required for high affinity TGF-beta binding: proteolytic cleavage separates the domains and inactivates the neutralizing activity of the soluble receptor
    • Mendoza V., Vilchis-Landeros M.M., Mendoza-Hernandez G., Huang T., Villarreal M.M., Hinck A.P., Lopez-Casillas F., Montiel J.L. Betaglycan has two independent domains required for high affinity TGF-beta binding: proteolytic cleavage separates the domains and inactivates the neutralizing activity of the soluble receptor. Biochemistry 2009, 48:11755-11765.
    • (2009) Biochemistry , vol.48 , pp. 11755-11765
    • Mendoza, V.1    Vilchis-Landeros, M.M.2    Mendoza-Hernandez, G.3    Huang, T.4    Villarreal, M.M.5    Hinck, A.P.6    Lopez-Casillas, F.7    Montiel, J.L.8
  • 45
    • 0035816662 scopus 로고    scopus 로고
    • Functional roles for the cytoplasmic domain of the type III transforming growth factor beta receptor in regulating transforming growth factor beta signaling
    • Blobe G.C., Schiemann W.P., Pepin M.C., Beauchemin M., Moustakas A., Lodish H.F., O'Connor-McCourt M.D. Functional roles for the cytoplasmic domain of the type III transforming growth factor beta receptor in regulating transforming growth factor beta signaling. J. Biol. Chem. 2001, 276:24627-24637.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24627-24637
    • Blobe, G.C.1    Schiemann, W.P.2    Pepin, M.C.3    Beauchemin, M.4    Moustakas, A.5    Lodish, H.F.6    O'Connor-McCourt, M.D.7
  • 46
    • 66249141288 scopus 로고    scopus 로고
    • The type III TGF-beta receptor regulates epithelial and cancer cell migration through beta-arrestin2-mediated activation of Cdc42
    • Mythreye K., Blobe G.C. The type III TGF-beta receptor regulates epithelial and cancer cell migration through beta-arrestin2-mediated activation of Cdc42. Proc. Natl Acad. Sci. USA 2009, 106:8221-8226.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 8221-8226
    • Mythreye, K.1    Blobe, G.C.2
  • 47
    • 69449101160 scopus 로고    scopus 로고
    • The type III transforming growth factor-beta receptor negatively regulates nuclear factor kappa B signaling through its interaction with beta-arrestin2
    • You H.J., How T., Blobe G.C. The type III transforming growth factor-beta receptor negatively regulates nuclear factor kappa B signaling through its interaction with beta-arrestin2. Carcinogenesis 2009, 30:1281-1287.
    • (2009) Carcinogenesis , vol.30 , pp. 1281-1287
    • You, H.J.1    How, T.2    Blobe, G.C.3
  • 48
    • 0035955713 scopus 로고    scopus 로고
    • A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC
    • Blobe G.C., Liu X., Fang S.J., How T., Lodish H.F. A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC. J. Biol. Chem. 2001, 276:39608-39617.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39608-39617
    • Blobe, G.C.1    Liu, X.2    Fang, S.J.3    How, T.4    Lodish, H.F.5
  • 50
    • 58049195151 scopus 로고    scopus 로고
    • Endocytosis of the type III transforming growth factor-beta (TGF-beta) receptor through the clathrin-independent/lipid raft pathway regulates TGF-beta signaling and receptor down-regulation
    • Finger E.C., Lee N.Y., You H.J., Blobe G.C. Endocytosis of the type III transforming growth factor-beta (TGF-beta) receptor through the clathrin-independent/lipid raft pathway regulates TGF-beta signaling and receptor down-regulation. J. Biol. Chem. 2008, 283:34808-34818.
    • (2008) J. Biol. Chem. , vol.283 , pp. 34808-34818
    • Finger, E.C.1    Lee, N.Y.2    You, H.J.3    Blobe, G.C.4
  • 51
    • 77954480793 scopus 로고    scopus 로고
    • TGF beta (transforming growth factor beta) receptor type III directs clathrin-mediated endocytosis of TGF beta receptor types I and II, Biochem J 429
    • S. McLean, G.M. Di Guglielmo, TGF beta (transforming growth factor beta) receptor type III directs clathrin-mediated endocytosis of TGF beta receptor types I and II, Biochem J 429 (2010) 137-145.
    • (2010) , pp. 137-145
    • McLean, S.1    Di Guglielmo, G.M.2
  • 52
    • 0037099745 scopus 로고    scopus 로고
    • TGF-beta receptor-activated p38 MAP kinase mediates Smad-independent TGF-beta responses
    • Yu L., Hebert M.C., Zhang Y.E. TGF-beta receptor-activated p38 MAP kinase mediates Smad-independent TGF-beta responses. EMBO J. 2002, 21:3749-3759.
    • (2002) EMBO J. , vol.21 , pp. 3749-3759
    • Yu, L.1    Hebert, M.C.2    Zhang, Y.E.3
  • 53
    • 1942501852 scopus 로고    scopus 로고
    • Syndecan-2 regulates transforming growth factor-beta signaling
    • Chen L., Klass C., Woods A. Syndecan-2 regulates transforming growth factor-beta signaling. J. Biol. Chem. 2004, 279:15715-15718.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15715-15718
    • Chen, L.1    Klass, C.2    Woods, A.3
  • 55
    • 77955244326 scopus 로고    scopus 로고
    • gamma-secretase-dependent cleavage initiates notch signaling from the plasma membrane, Traffic 11
    • E.B. Sorensen, S.D. Conner, gamma-secretase-dependent cleavage initiates notch signaling from the plasma membrane, Traffic 11 (2010) 1234-1245.
    • (2010) , pp. 1234-1245
    • Sorensen, E.B.1    Conner, S.D.2
  • 57
    • 34249664257 scopus 로고    scopus 로고
    • The insulin-like growth factor 1 (IGF-1) receptor is a substrate for gamma-secretase-mediated intramembrane proteolysis
    • McElroy B., Powell J.C., McCarthy J.V. The insulin-like growth factor 1 (IGF-1) receptor is a substrate for gamma-secretase-mediated intramembrane proteolysis. Biochem. Biophys. Res. Commun. 2007, 358:1136-1141.
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , pp. 1136-1141
    • McElroy, B.1    Powell, J.C.2    McCarthy, J.V.3
  • 58
    • 33749072714 scopus 로고    scopus 로고
    • Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain
    • Sardi S.P., Murtie J., Koirala S., Patten B.A., Corfas G. Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain. Cell 2006, 127:185-197.
    • (2006) Cell , vol.127 , pp. 185-197
    • Sardi, S.P.1    Murtie, J.2    Koirala, S.3    Patten, B.A.4    Corfas, G.5
  • 59
    • 1542677095 scopus 로고    scopus 로고
    • Syndecan 3 intramembrane proteolysis is presenilin/gamma-secretase-dependent and modulates cytosolic signaling
    • Schulz J.G., Annaert W., Vandekerckhove J., Zimmermann P., De Strooper B., David G. Syndecan 3 intramembrane proteolysis is presenilin/gamma-secretase-dependent and modulates cytosolic signaling. J. Biol. Chem. 2003, 278:48651-48657.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48651-48657
    • Schulz, J.G.1    Annaert, W.2    Vandekerckhove, J.3    Zimmermann, P.4    De Strooper, B.5    David, G.6
  • 60
    • 0033639117 scopus 로고    scopus 로고
    • Requirements for presenilin-dependent cleavage of Notch and other transmembrane proteins
    • Struhl G., Adachi A. Requirements for presenilin-dependent cleavage of Notch and other transmembrane proteins. Mol. Cell 2000, 6:625-636.
    • (2000) Mol. Cell , vol.6 , pp. 625-636
    • Struhl, G.1    Adachi, A.2
  • 61
    • 77954367715 scopus 로고    scopus 로고
    • The p75NTR intracellular domain generated by neurotrophin-induced receptor cleavage potentiates Trk signaling, J Cell Sci 123
    • C. Ceni, R.P. Kommaddi, R. Thomas, E. Vereker, X. Liu, P.S. McPherson, B. Ritter, P.A. Barker, The p75NTR intracellular domain generated by neurotrophin-induced receptor cleavage potentiates Trk signaling, J Cell Sci 123 (2010) 2299-2307.
    • (2010) , pp. 2299-2307
    • Ceni, C.1    Kommaddi, R.P.2    Thomas, R.3    Vereker, E.4    Liu, X.5    McPherson, P.S.6    Ritter, B.7    Barker, P.A.8
  • 62
    • 0036727125 scopus 로고    scopus 로고
    • Gamma-secretase-mediated proteolysis in cell-surface-receptor signalling
    • Fortini M.E. Gamma-secretase-mediated proteolysis in cell-surface-receptor signalling. Nat. Rev. Mol. Cell Biol. 2002, 3:673-684.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 673-684
    • Fortini, M.E.1
  • 63
    • 54949110552 scopus 로고    scopus 로고
    • Proteomic profiling of gamma-secretase substrates and mapping of substrate requirements
    • Hemming M.L., Elias J.E., Gygi S.P., Selkoe D.J. Proteomic profiling of gamma-secretase substrates and mapping of substrate requirements. PLoS Biol. 2008, 6:e257.
    • (2008) PLoS Biol. , vol.6
    • Hemming, M.L.1    Elias, J.E.2    Gygi, S.P.3    Selkoe, D.J.4
  • 65
    • 0024792629 scopus 로고
    • Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta
    • Andres J.L., Stanley K., Cheifetz S., Massague J. Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta. J. Cell Biol. 1989, 109:3137-3145.
    • (1989) J. Cell Biol. , vol.109 , pp. 3137-3145
    • Andres, J.L.1    Stanley, K.2    Cheifetz, S.3    Massague, J.4
  • 67
    • 0026646785 scopus 로고
    • Endoglin is a component of the transforming growth factor-beta receptor system in human endothelial cells
    • Cheifetz S., Bellon T., Cales C., Vera S., Bernabeu C., Massague J., Letarte M. Endoglin is a component of the transforming growth factor-beta receptor system in human endothelial cells. J. Biol. Chem. 1992, 267:19027-19030.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19027-19030
    • Cheifetz, S.1    Bellon, T.2    Cales, C.3    Vera, S.4    Bernabeu, C.5    Massague, J.6    Letarte, M.7
  • 68
    • 0025310515 scopus 로고
    • Primary structure of endoglin, an RGD-containing glycoprotein of human endothelial cells
    • Gougos A., Letarte M. Primary structure of endoglin, an RGD-containing glycoprotein of human endothelial cells. J. Biol. Chem. 1990, 265:8361-8364.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8361-8364
    • Gougos, A.1    Letarte, M.2
  • 69
    • 0034701244 scopus 로고    scopus 로고
    • Expression analysis of endoglin missense and truncation mutations: insights into protein structure and disease mechanisms
    • Lux A., Gallione C.J., Marchuk D.A. Expression analysis of endoglin missense and truncation mutations: insights into protein structure and disease mechanisms. Hum. Mol. Genet. 2000, 9:745-755.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 745-755
    • Lux, A.1    Gallione, C.J.2    Marchuk, D.A.3
  • 73
    • 33646089201 scopus 로고    scopus 로고
    • Hereditary hemorrhagic telangiectasia, a vascular dysplasia affecting the TGF-beta signaling pathway
    • Fernandez L.A., Sanz-Rodriguez F., Blanco F.J., Bernabeu C., Botella L.M. Hereditary hemorrhagic telangiectasia, a vascular dysplasia affecting the TGF-beta signaling pathway. Clin. Med. Res. 2006, 4:66-78.
    • (2006) Clin. Med. Res. , vol.4 , pp. 66-78
    • Fernandez, L.A.1    Sanz-Rodriguez, F.2    Blanco, F.J.3    Bernabeu, C.4    Botella, L.M.5
  • 74
    • 3042589327 scopus 로고    scopus 로고
    • Endoglin controls cell migration and composition of focal adhesions: function of the cytosolic domain
    • Conley B.A., Koleva R., Smith J.D., Kacer D., Zhang D., Bernabeu C., Vary C.P. Endoglin controls cell migration and composition of focal adhesions: function of the cytosolic domain. J. Biol. Chem. 2004, 279:27440-27449.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27440-27449
    • Conley, B.A.1    Koleva, R.2    Smith, J.D.3    Kacer, D.4    Zhang, D.5    Bernabeu, C.6    Vary, C.P.7
  • 75
    • 0033601179 scopus 로고    scopus 로고
    • Interdependent SMAD and JNK signaling in transforming growth factor-beta-mediated transcription
    • Engel M.E., McDonnell M.A., Law B.K., Moses H.L. Interdependent SMAD and JNK signaling in transforming growth factor-beta-mediated transcription. J. Biol. Chem. 1999, 274:37413-37420.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37413-37420
    • Engel, M.E.1    McDonnell, M.A.2    Law, B.K.3    Moses, H.L.4
  • 76
    • 0034634656 scopus 로고    scopus 로고
    • Requirement of Ras/MAPK pathway activation by transforming growth factor beta for transforming growth factor beta 1 production in a Smad-dependent pathway
    • Yue J., Mulder K.M. Requirement of Ras/MAPK pathway activation by transforming growth factor beta for transforming growth factor beta 1 production in a Smad-dependent pathway. J. Biol. Chem. 2000, 275:35656.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35656
    • Yue, J.1    Mulder, K.M.2
  • 77
    • 37549057010 scopus 로고    scopus 로고
    • Transforming growth factor-beta-activated protein kinase 1-binding protein (TAB)-1alpha, but not TAB1beta, mediates cytokine-induced p38 mitogen-activated protein kinase phosphorylation and cell death in insulin-producing cells
    • Makeeva N., Roomans G.M., Myers J.W., Welsh N. Transforming growth factor-beta-activated protein kinase 1-binding protein (TAB)-1alpha, but not TAB1beta, mediates cytokine-induced p38 mitogen-activated protein kinase phosphorylation and cell death in insulin-producing cells. Endocrinology 2008, 149:302-309.
    • (2008) Endocrinology , vol.149 , pp. 302-309
    • Makeeva, N.1    Roomans, G.M.2    Myers, J.W.3    Welsh, N.4


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