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Volumn 14, Issue 3, 2004, Pages 236-241

Diverse Substrate Recognition Mechanisms for Rhomboids: Thrombomodulin Is Cleaved by Mammalian Rhomboids

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; MAMMALIA; VERTEBRATA;

EID: 1242288387     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(04)00008-9     Document Type: Article
Times cited : (132)

References (21)
  • 1
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila Rhomboid-1 defines a family of putative intramembrane serine proteases
    • Urban S., Lee J.R., Freeman M. Drosophila Rhomboid-1 defines a family of putative intramembrane serine proteases. Cell. 107:2001;173-182.
    • (2001) Cell , vol.107 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 2
    • 0037102238 scopus 로고    scopus 로고
    • A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands
    • Urban S., Lee J.R., Freeman M. A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands. EMBO J. 21:2002;4277-4286.
    • (2002) EMBO J. , vol.21 , pp. 4277-4286
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 3
    • 0037015265 scopus 로고    scopus 로고
    • Conservation of intramembrane proteolytic activity and substrate specificity in prokaryotic and eukaryotic rhomboids
    • Urban S., Schlieper D., Freeman M. Conservation of intramembrane proteolytic activity and substrate specificity in prokaryotic and eukaryotic rhomboids. Curr. Biol. 12:2002;1507-1512.
    • (2002) Curr. Biol. , vol.12 , pp. 1507-1512
    • Urban, S.1    Schlieper, D.2    Freeman, M.3
  • 4
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • McQuibban G.A., Saurya S., Freeman M. Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature. 423:2003;537-541.
    • (2003) Nature , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 5
    • 0037126036 scopus 로고    scopus 로고
    • A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes
    • Gallio M., Sturgill G., Rather P., Kylsten P. A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes. Proc. Natl. Acad. Sci. USA. 99:2002;12208-12213.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12208-12213
    • Gallio, M.1    Sturgill, G.2    Rather, P.3    Kylsten, P.4
  • 6
    • 0036424840 scopus 로고    scopus 로고
    • A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1
    • Esser K., Tursun B., Ingenhoven M., Michaelis G., Pratje E. A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1. J. Mol. Biol. 323:2002;835-843.
    • (2002) J. Mol. Biol. , vol.323 , pp. 835-843
    • Esser, K.1    Tursun, B.2    Ingenhoven, M.3    Michaelis, G.4    Pratje, E.5
  • 7
    • 0043095416 scopus 로고    scopus 로고
    • Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion
    • Sesaki H., Southard S.M., Hobbs A.E., Jensen R.E. Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion. Biochem. Biophys. Res. Commun. 308:2003;276-283.
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 276-283
    • Sesaki, H.1    Southard, S.M.2    Hobbs, A.E.3    Jensen, R.E.4
  • 8
    • 0042526632 scopus 로고    scopus 로고
    • Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
    • Herlan M., Vogel F., Bornhovd C., Neupert W., Reichert A.S. Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J. Biol. Chem. 278:2003;27781-27788.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27781-27788
    • Herlan, M.1    Vogel, F.2    Bornhovd, C.3    Neupert, W.4    Reichert, A.S.5
  • 10
    • 0035913906 scopus 로고    scopus 로고
    • Regulated intracellular ligand transport and proteolysis controls EGF signal activation in Drosophila
    • Lee J.R., Urban S., Garvey C.F., Freeman M. Regulated intracellular ligand transport and proteolysis controls EGF signal activation in Drosophila. Cell. 107:2001;161-171.
    • (2001) Cell , vol.107 , pp. 161-171
    • Lee, J.R.1    Urban, S.2    Garvey, C.F.3    Freeman, M.4
  • 11
    • 0038771224 scopus 로고    scopus 로고
    • Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain
    • Urban S., Freeman M. Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain. Mol. Cell. 11:2003;1425-1434.
    • (2003) Mol. Cell , vol.11 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 12
    • 0036719236 scopus 로고    scopus 로고
    • New mechanisms for vascular control of inflammation mediated by natural anticoagulant proteins
    • Esmon C.T. New mechanisms for vascular control of inflammation mediated by natural anticoagulant proteins. J. Exp. Med. 196:2002;561-564.
    • (2002) J. Exp. Med. , vol.196 , pp. 561-564
    • Esmon, C.T.1
  • 13
    • 0032537494 scopus 로고    scopus 로고
    • Characterization of a mammalian cDNA encoding a protein with high sequence similarity to the Drosophila regulatory protein Rhomboid
    • Pascall J.C., Brown K.D. Characterization of a mammalian cDNA encoding a protein with high sequence similarity to the Drosophila regulatory protein Rhomboid. FEBS Lett. 429:1998;337-340.
    • (1998) FEBS Lett. , vol.429 , pp. 337-340
    • Pascall, J.C.1    Brown, K.D.2
  • 14
    • 0029790055 scopus 로고    scopus 로고
    • The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex
    • Stearns-Kurosawa D.J., Kurosawa S., Mollica J.S., Ferrell G.L., Esmon C.T. The endothelial cell protein C receptor augments protein C activation by the thrombin-thrombomodulin complex. Proc. Natl. Acad. Sci. USA. 93:1996;10212-10216.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10212-10216
    • Stearns-Kurosawa, D.J.1    Kurosawa, S.2    Mollica, J.S.3    Ferrell, G.L.4    Esmon, C.T.5
  • 15
    • 0027245963 scopus 로고
    • Pref-1, a protein containing EGF-like repeats, inhibits adipocyte differentiation
    • Smas C.M., Sul H.S. Pref-1, a protein containing EGF-like repeats, inhibits adipocyte differentiation. Cell. 73:1993;725-734.
    • (1993) Cell , vol.73 , pp. 725-734
    • Smas, C.M.1    Sul, H.S.2
  • 16
    • 0036127811 scopus 로고    scopus 로고
    • Cloning and expression of Ventrhoid, a novel vertebrate homologue of the Drosophila EGF pathway gene rhomboid
    • Jaszai J., Brand M. Cloning and expression of Ventrhoid, a novel vertebrate homologue of the Drosophila EGF pathway gene rhomboid. Mech. Dev. 113:2002;73-77.
    • (2002) Mech. Dev. , vol.113 , pp. 73-77
    • Jaszai, J.1    Brand, M.2
  • 17
    • 0025241217 scopus 로고
    • Plasma thrombomodulin in health and diseases
    • Takano S., Kimura S., Ohdama S., Aoki N. Plasma thrombomodulin in health and diseases. Blood. 76:1990;2024-2029.
    • (1990) Blood , vol.76 , pp. 2024-2029
    • Takano, S.1    Kimura, S.2    Ohdama, S.3    Aoki, N.4
  • 18
    • 0030066667 scopus 로고    scopus 로고
    • Release of thrombomodulin from endothelial cells by concerted action of TNF-alpha and neutrophils: In vivo and in vitro studies
    • Boehme M.W., Deng Y., Raeth U., Bierhaus A., Ziegler R., Stremmel W., Nawroth P.P. Release of thrombomodulin from endothelial cells by concerted action of TNF-alpha and neutrophils. in vivo and in vitro studies Immunology. 87:1996;134-140.
    • (1996) Immunology , vol.87 , pp. 134-140
    • Boehme, M.W.1    Deng, Y.2    Raeth, U.3    Bierhaus, A.4    Ziegler, R.5    Stremmel, W.6    Nawroth, P.P.7
  • 19
    • 0034234250 scopus 로고    scopus 로고
    • A family of rhomboid-like genes: Drosophila rhomboid-1 and roughoid/rhomboid-3 cooperate to activate EGF receptor signalling
    • Wasserman J.D., Urban S., Freeman M. A family of rhomboid-like genes. Drosophila rhomboid-1 and roughoid/rhomboid-3 cooperate to activate EGF receptor signalling Genes Dev. 14:2000;1651-1663.
    • (2000) Genes Dev. , vol.14 , pp. 1651-1663
    • Wasserman, J.D.1    Urban, S.2    Freeman, M.3
  • 20
    • 0034667916 scopus 로고    scopus 로고
    • Brother of rhomboid, a rhomboid-related gene expressed during early Drosophila oogenesis, promotes EGF-R/MAPK signaling
    • Guichard A., Roark M., Ronshaugen M., Bier E. brother of rhomboid, a rhomboid-related gene expressed during early Drosophila oogenesis, promotes EGF-R/MAPK signaling. Dev. Biol. 226:2000;255-266.
    • (2000) Dev. Biol. , vol.226 , pp. 255-266
    • Guichard, A.1    Roark, M.2    Ronshaugen, M.3    Bier, E.4
  • 21
    • 0037264371 scopus 로고    scopus 로고
    • The rhomboids: A nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers
    • Koonin E.V., Makarova K.S., Rogozin I.B., Davidovic L., Letellier M.C., Pellegrini L. The rhomboids. a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers Genome Biol. 4:2003;R19.
    • (2003) Genome Biol. , vol.4 , pp. 19
    • Koonin, E.V.1    Makarova, K.S.2    Rogozin, I.B.3    Davidovic, L.4    Letellier, M.C.5    Pellegrini, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.