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Volumn 5, Issue 3, 2004, Pages 188-197

Proteolysis within the membrane: Rhomboids revealed

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; GROWTH FACTOR; SERINE PROTEINASE;

EID: 1542374120     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1334     Document Type: Review
Times cited : (60)

References (107)
  • 1
    • 0014201592 scopus 로고
    • Three-dimensional structure of tosyl-α-chymotrypsin
    • Matthews, B. W., Sigler, P. B., Henderson, R. & Blow, D. M. Three-dimensional structure of tosyl-α-chymotrypsin. Nature 214, 652-656 (1967).
    • (1967) Nature , vol.214 , pp. 652-656
    • Matthews, B.W.1    Sigler, P.B.2    Henderson, R.3    Blow, D.M.4
  • 3
    • 0031301274 scopus 로고    scopus 로고
    • Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs
    • Rawson, R. B. et al. Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs. Mol. Cell 1, 47-57 (1997).
    • (1997) Mol. Cell , vol.1 , pp. 47-57
    • Rawson, R.B.1
  • 4
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M. S. et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517 (1999).
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 5
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li, Y. M. et al. Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405, 689-694 (2000).
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.M.1
  • 6
    • 0033780472 scopus 로고    scopus 로고
    • Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
    • Esler, W. P. et al. Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1. Nature Cell Biol. 2, 428-434(2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 428-434
    • Esler, W.P.1
  • 7
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofn, A., Binns, K., Lemberg, M. K., Ashman, K. & Martoglio, B. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296, 2215-2218 (2002).
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofn, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 8
    • 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, 173-182 (2001). This paper reports the discovery that rhomboids are a new, conserved family of intramembrane serine proteases.
    • (2001) Cell , vol.107 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 9
    • 0034234250 scopus 로고    scopus 로고
    • A family of rhomboid-like genes: Drosophila rhomboid-1 and roughoid/rhombcid-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/rhombcid-3 cooperate to activate EGF receptor signalling. Genes Dev. 14, 1651-1663 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 1651-1663
    • Wasserman, J.D.1    Urban, S.2    Freeman, M.3
  • 10
    • 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, 255-266 (2000).
    • (2000) Dev. Biol. , vol.226 , pp. 255-266
    • Guichard, A.1    Roark, M.2    Ronshaugen, M.3    Bier, E.4
  • 11
    • 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. et al. The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers. Genome Biol. 4, R19 (2003). This paper describes a detailed phylogenetic analysis of rhomboids and points out that they are the most widely conserved polytopic, membrane proteins.
    • (2003) Genome Biol. , vol.4
    • Koonin, E.V.1
  • 12
    • 34250134008 scopus 로고
    • Mutations affecting the pattem of the larval cuticle in Drosophila melanogaster. II. Zygotic loci on the third chromosome
    • Jürgene, G., Wieschaus, E, Nüsslein-Volhard, C. & Kluding, H. Mutations affecting the pattem of the larval cuticle in Drosophila melanogaster. II. Zygotic loci on the third chromosome. Wilhelm Roux's Arch. Dev. Biol. 193, 283-295 (1984).
    • (1984) Wilhelm Roux's Arch. Dev. Biol. , vol.193 , pp. 283-295
    • Jürgene, G.1    Wieschaus, E.2    Nüsslein-Volhard, C.3    Kluding, H.4
  • 13
    • 0024114027 scopus 로고
    • A group of genes required for pattern formation in the ventral ectoderm of the Drosophila embryo
    • Mayer, U. & Nüsslein-Volhard, C. A group of genes required for pattern formation in the ventral ectoderm of the Drosophila embryo. Genes Dev. 2, 1496-1511 (1988).
    • (1988) Genes Dev. , vol.2 , pp. 1496-1511
    • Mayer, U.1    Nüsslein-Volhard, C.2
  • 14
    • 0031005779 scopus 로고    scopus 로고
    • A thousand and one roles for the Drosophila EGF receptor
    • Schweitzer, R. & Shilo, B.-Z. A thousand and one roles for the Drosophila EGF receptor. Trends Genet. 13, 191-196 (1997).
    • (1997) Trends Genet. , vol.13 , pp. 191-196
    • Schweitzer, R.1    Shilo, B.-Z.2
  • 16
    • 0026459770 scopus 로고
    • Identifying targets of the rough homeobox gene of Drosophila: Evidence that rhomboid functions in eye development
    • Freeman, M., Kimmel, B. E. & Rubin, G. M. Identifying targets of the rough homeobox gene of Drosophila: evidence that rhomboid functions in eye development. Development 116, 335-346 (1992).
    • (1992) Development , vol.116 , pp. 335-346
    • Freeman, M.1    Kimmel, B.E.2    Rubin, G.M.3
  • 17
    • 0025060344 scopus 로고
    • Rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster
    • Bier, E., Jan, L. Y. & Jan, Y. N. rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster. Genes Dev. 4, 190-203 (1990).
    • (1990) Genes Dev. , vol.4 , pp. 190-203
    • Bier, E.1    Jan, L.Y.2    Jan, Y.N.3
  • 18
    • 0027176294 scopus 로고
    • The Drosophila rhomboid gene mediates the localized formation of wing veins and interacts genetically with components of the EGF-R signaling pathway
    • Sturtevant, M. A., Roark, M. & Bier, E. The Drosophila rhomboid gene mediates the localized formation of wing veins and interacts genetically with components of the EGF-R signaling pathway. Genes Dev. 7, 961-973 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 961-973
    • Sturtevant, M.A.1    Roark, M.2    Bier, E.3
  • 19
    • 0027157553 scopus 로고
    • Spatially localized rhomboid is required for establishment of the dorsal-ventral axis in Drosophila oogenesis
    • Ruohola-Baker, H. et al. Spatially localized rhomboid is required for establishment of the dorsal-ventral axis in Drosophila oogenesis. Cell 73, 953-965 (1993).
    • (1993) Cell , vol.73 , pp. 953-965
    • Ruohola-Baker, H.1
  • 20
    • 0028059268 scopus 로고
    • The spitz gene is required for photoreceptor determination in the Drosophila eye where it interacts with the EGF receptor
    • Freeman, M. The spitz gene is required for photoreceptor determination in the Drosophila eye where it interacts with the EGF receptor. Mech. Mach. Dev 48, 25-33 (1994).
    • (1994) Mech. Mach. Dev. , vol.48 , pp. 25-33
    • Freeman, M.1
  • 21
    • 0037429688 scopus 로고    scopus 로고
    • Signaling by the Drosophila epidermal growth factor receptor pathway during development
    • Shilo, B. Z. Signaling by the Drosophila epidermal growth factor receptor pathway during development. Exp. Cell Res. 284, 140-149 (2003).
    • (2003) Exp. Cell Res. , vol.284 , pp. 140-149
    • Shilo, B.Z.1
  • 22
    • 0029855245 scopus 로고    scopus 로고
    • The Drosophila embryonic midline is the site of Spitz processing, and induces activation of the EGF receptor in the ventral ectoderm
    • Golembo, M., Raz, E. & Shilo, B. Z. The Drosophila embryonic midline is the site of Spitz processing, and induces activation of the EGF receptor in the ventral ectoderm. Development 122, 3363-3370 (1996).
    • (1996) Development , vol.122 , pp. 3363-3370
    • Golembo, M.1    Raz, E.2    Shilo, B.Z.3
  • 23
    • 0032774518 scopus 로고    scopus 로고
    • Rhomboid and Star interact synergistically to promote EGFR/MAPK signaling during Drosophila wing vein development
    • Guichard, A. et al. rhomboid and Star interact synergistically to promote EGFR/MAPK signaling during Drosophila wing vein development. Development 126, 2663-2676 (1999). An elegant genetic demonstration that D. melanogaster Rhomboid-1 and Star function co-dependently to activate EGFR signalling.
    • (1999) Development , vol.126 , pp. 2663-2676
    • Guichard, A.1
  • 24
    • 0032582797 scopus 로고    scopus 로고
    • An autoregulatory cascade of EGF receptor signalling patterns the Drosophila egg
    • Wasserman, J. D. & Freeman, M. An autoregulatory cascade of EGF receptor signalling patterns the Drosophila egg. Cell 95, 355-364 (1998).
    • (1998) Cell , vol.95 , pp. 355-364
    • Wasserman, J.D.1    Freeman, M.2
  • 25
    • 0031092699 scopus 로고    scopus 로고
    • Requirement for EGF receptor signalling in neural recruitment during formation of Drosophila chordotonal sense organ clusters
    • zür Lage, P., Jan, Y. N. & Jarman, A. P. Requirement for EGF receptor signalling in neural recruitment during formation of Drosophila chordotonal sense organ clusters. Curr. Biol. 7, 166-175 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 166-175
    • Zür Lage, P.1    Jan, Y.N.2    Jarman, A.P.3
  • 26
    • 0033678762 scopus 로고    scopus 로고
    • Regulation of Drosophila wing vein patterning: Net encodes a bHLH protein repressing rhomboid and is repressed by rhomboid-dependent Egfr signalling
    • Brentrup, D., Lerch, H., Jackle, H. & Noll, M. Regulation of Drosophila wing vein patterning: net encodes a bHLH protein repressing rhomboid and is repressed by rhomboid-dependent Egfr signalling. Development 127, 4729-4741 (2000).
    • (2000) Development , vol.127 , pp. 4729-4741
    • Brentrup, D.1    Lerch, H.2    Jackle, H.3    Noll, M.4
  • 27
    • 0030866482 scopus 로고    scopus 로고
    • In situ activation pattern of Drosophila EGF receptor pathway during development
    • Gabay, L., Seger, R. & Shilo, B.-Z. In situ activation pattern of Drosophila EGF receptor pathway during development. Science 277, 1103-1106 (1997).
    • (1997) Science , vol.277 , pp. 1103-1106
    • Gabay, L.1    Seger, R.2    Shilo, B.-Z.3
  • 28
    • 0028142324 scopus 로고
    • New functions of the Drosophila rhomboid gene during embryonic and adult development are revealed by a novel genetic method, enhancer piracy
    • Noll, R., Sturtevant, M. A., Gollapudi, R. R. & Bier, E. New functions of the Drosophila rhomboid gene during embryonic and adult development are revealed by a novel genetic method, enhancer piracy. Development 120, 2329-2338 (1994).
    • (1994) Development , vol.120 , pp. 2329-2338
    • Noll, R.1    Sturtevant, M.A.2    Gollapudi, R.R.3    Bier, E.4
  • 29
    • 0028954113 scopus 로고
    • Analysis of the genetic hierarchy guiding wing vein development in Drosophila
    • Sturtevant, M. A. & Bier, E. Analysis of the genetic hierarchy guiding wing vein development in Drosophila. Development 121, 785-801 (1995).
    • (1995) Development , vol.121 , pp. 785-801
    • Sturtevant, M.A.1    Bier, E.2
  • 30
    • 0028363844 scopus 로고
    • Characterization of Star and its interactions with sevenless and EGF receptor during photoreceptor cell development in Drosophila
    • Kolodkin, A. L, Pickup, A. T., Lin, D. M., Goodman, C. S. & Banerjee, U. Characterization of Star and its interactions with sevenless and EGF receptor during photoreceptor cell development in Drosophila. Development 120, 1731-1745 (1994).
    • (1994) Development , vol.120 , pp. 1731-1745
    • Kolodkin, A.L.1    Pickup, A.T.2    Lin, D.M.3    Goodman, C.S.4    Banerjee, U.5
  • 31
    • 0034650255 scopus 로고    scopus 로고
    • Rhomboid and Star facilitate presentation and processing of the Drosophila TGF-α homolog Spitz
    • Bang, A. G. & Kintner, C. Rhomboid and Star facilitate presentation and processing of the Drosophila TGF-α homolog Spitz. Genes Dev. 14, 177-186 (2000). The first experimental demonstration that Star and Rhomboid-1 somehow trigger the proteolytoc release of Spitz.
    • (2000) Genes Dev. , vol.14 , pp. 177-186
    • Bang, A.G.1    Kintner, C.2
  • 32
    • 0027443215 scopus 로고
    • Star is required for neuronal differentiation in the Drosophila retina and displays dosage-sensitive interactions with Ras 1
    • Heberlein, U., Hariharan, I. K. & Rubin, G. M. Star is required for neuronal differentiation in the Drosophila retina and displays dosage-sensitive interactions with Ras 1. Dev. Biol. 160, 51-63 (1993).
    • (1993) Dev. Biol. , vol.160 , pp. 51-63
    • Heberlein, U.1    Hariharan, I.K.2    Rubin, G.M.3
  • 33
    • 0033555978 scopus 로고    scopus 로고
    • The role of Star in the production of an activated ligand for the EGF receptor signaling pathway
    • Pickup, A. T. & Banerjee, U. The role of Star in the production of an activated ligand for the EGF receptor signaling pathway. Dev Biol. 205, 254-259 (1999).
    • (1999) Dev Biol. , vol.205 , pp. 254-259
    • Pickup, A.T.1    Banerjee, U.2
  • 34
    • 0034889139 scopus 로고    scopus 로고
    • Function of the Drosophila TGF-α homolog Spitz is controlled by Star and interacts directly with Star
    • Hsiung, F., Griffis, E. R., Pickup, A., Powers, M. A. & Moses, K. Function of the Drosophila TGF-α homolog Spitz is controlled by Star and interacts directly with Star. Mech. Dev. 107, 13-23 (2001).
    • (2001) Mech. Dev. , vol.107 , pp. 13-23
    • Hsiung, F.1    Griffis, E.R.2    Pickup, A.3    Powers, M.A.4    Moses, K.5
  • 35
    • 0032715588 scopus 로고    scopus 로고
    • Rhomboid function in the midline of the Drosophila CNS
    • Lanoue, B. R. & Jacobs, J. R. Rhomboid function in the midline of the Drosophila CNS. Dev. Genet. 25, 321-330 (1999).
    • (1999) Dev. Genet. , vol.25 , pp. 321-330
    • Lanoue, B.R.1    Jacobs, J.R.2
  • 36
    • 0031931299 scopus 로고    scopus 로고
    • Sequential activation of the EGF receptor pathway during Drosophila oogenesis establishes the dorsoventral axis
    • Sapir, A., Schweitzer, R. & Shilo, B.-Z. Sequential activation of the EGF receptor pathway during Drosophila oogenesis establishes the dorsoventral axis. Development 125, 191-200 (1998).
    • (1998) Development , vol.125 , pp. 191-200
    • Sapir, A.1    Schweitzer, R.2    Shilo, B.-Z.3
  • 37
    • 0029015431 scopus 로고
    • Secreted Spitz triggers the DER signalling pathway and is a limiting component in embryonic ventral ectoderm determination
    • Schweitzer, R., Shaharabany, M., Seger, R. & Shilo, B.-Z. Secreted Spitz triggers the DER signalling pathway and is a limiting component in embryonic ventral ectoderm determination, Genes Dev. 9, 1518-1529 (1995). Reported that the soluble form of Spitz was active but that the membrane-tethered form had no detectable activity, this led to the idea that proteolysis of Spitz is a key step in EGFR activation.
    • (1995) Genes Dev. , vol.9 , pp. 1518-1529
    • Schweitzer, R.1    Shaharabany, M.2    Seger, R.3    Shilo, B.-Z.4
  • 38
    • 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, 161-171 (2001). This paper was the first to describe the mechanism by which Star and Rhomboid-1 control the trafficking and cleavage of the TGFα-like growth factor Spitz.
    • (2001) Cell , vol.107 , pp. 161-171
    • Lee, J.R.1    Urban, S.2    Garvey, C.F.3    Freeman, M.4
  • 39
    • 0036339998 scopus 로고    scopus 로고
    • Mechanism of activation of the Drosophila EGF receptor by the TGRα ligand Gurken during oogenesis
    • Ghiglione, C. et al. Mechanism of activation of the Drosophila EGF receptor by the TGRα ligand Gurken during oogenesis. Development 129, 175-186 (2002).
    • (2002) Development , vol.129 , pp. 175-186
    • Ghiglione, C.1
  • 40
    • 0037080869 scopus 로고    scopus 로고
    • Intracellular trafficking by Star regulates cleavage of the Drosaphila EGF receptor ligand Spitz
    • Tsruya, R. et al. Intracellular trafficking by Star regulates cleavage of the Drosaphila EGF receptor ligand Spitz. Genes Dev. 16, 222-234 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 222-234
    • Tsruya, R.1
  • 41
    • 0037090712 scopus 로고    scopus 로고
    • Expression in mammalian cell cultures reveals interdependent, but distinct, functions for Star and Rhomboid proteins in the processing of the Drosophila transforming-growth-factor-α homologue Spitz
    • Pascall, J. C., Luck, J. E. & Brown, K. D. Expression in mammalian cell cultures reveals interdependent, but distinct, functions for Star and Rhomboid proteins in the processing of the Drosophila transforming-growth-factor-α homologue Spitz. Biochem. J. 363, 347-352 (2002).
    • (2002) Biochem. J. , vol.363 , pp. 347-352
    • Pascall, J.C.1    Luck, J.E.2    Brown, K.D.3
  • 42
    • 0034979828 scopus 로고    scopus 로고
    • PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and-2
    • Pellegrini, L. et al. PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and-2. J. Alzheimers Dis. 3, 181-190 (2001).
    • (2001) J. Alzheimers Dis. , vol.3 , pp. 181-190
    • Pellegrini, L.1
  • 43
    • 0031033450 scopus 로고    scopus 로고
    • Catalytic hydroxyl/amine dyads within serine proteases
    • Paetzel, M. & Dalbey, R. E. Catalytic hydroxyl/amine dyads within serine proteases. Trends Biochem. Sci. 22, 28-31 (1997).
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 28-31
    • Paetzel, M.1    Dalbey, R.E.2
  • 44
    • 0029072912 scopus 로고
    • Structural and functional roles of asparagine 175 in the cysteine protease papain
    • Vernet, T. et al. Structural and functional roles of asparagine 175 in the cysteine protease papain. J. Biol. Chem. 270, 16645-16652(1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 16645-16652
    • Vernet, T.1
  • 45
    • 0034625081 scopus 로고    scopus 로고
    • Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease
    • Ye, J., Dave, U. P., Grishin, N. V., Goldstein, J. L. & Brown, M. S. Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease. Proc. Natl Acad. Sci. USA 97, 5123-5128 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5123-5128
    • Ye, J.1    Dave, U.P.2    Grishin, N.V.3    Goldstein, J.L.4    Brown, M.S.5
  • 46
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch 1
    • Mumm, J. S. et al. A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch 1. Mol. Cell 5, 197-206 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 197-206
    • Mumm, J.S.1
  • 47
    • 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 6, 625-636 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 625-636
    • Struhl, G.1    Adachi, A.2
  • 48
    • 0036809216 scopus 로고    scopus 로고
    • Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis
    • Lemberg, M. K. & Martoglio, B. Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis. Mol. Cell 10, 735-744 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 735-744
    • Lemberg, M.K.1    Martoglio, B.2
  • 49
    • 0032185770 scopus 로고    scopus 로고
    • Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells
    • Sakai, J. et al. Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells. Mol. Cell 2, 505-514 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 505-514
    • Sakai, J.1
  • 50
    • 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, 1425-1434 (2003). This paper describes the requirements within the TMD of a rhomboid substrate that make it cleavable by rhomboids. It implies that destabilization of the TMD α-helix is necessary; it also predicts that a family of Toxoplasma gondii adhesion proteins are rhomboid substrates.
    • (2003) Mol. Cell , vol.11 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 51
    • 0034817498 scopus 로고    scopus 로고
    • Microneme proteins: Structural and functional requirements to promote adhesion and invasion by the apicomplexan parasite Toxoplasma gondii
    • Soldati, D., Dubremetz, J. F. & Lebrun, M. Microneme proteins: structural and functional requirements to promote adhesion and invasion by the apicomplexan parasite Toxoplasma gondii. Int. J. Parasitol. 31, 1293-1302 (2001).
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1293-1302
    • Soldati, D.1    Dubremetz, J.F.2    Lebrun, M.3
  • 52
    • 0037007235 scopus 로고    scopus 로고
    • Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii
    • Opitz, C. et al. Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii. EMBO J. 21, 1577-1585 (2002).
    • (2002) EMBO J. , vol.21 , pp. 1577-1585
    • Opitz, C.1
  • 53
    • 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, 4277-4286 (2002).
    • (2002) EMBO J. , vol.21 , pp. 4277-4286
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 54
    • 1242288387 scopus 로고    scopus 로고
    • Diverse substrate recognition mechanisms for rhomboids: Thrombomodulin is cleaved by mammalian rhomboids
    • Lohi, O., Urban, S. & Freeman, M. Diverse substrate recognition mechanisms for rhomboids: thrombomodulin is cleaved by mammalian rhomboids. Curr. Biol. 14, 263-241 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 263-241
    • Lohi, O.1    Urban, S.2    Freeman, M.3
  • 55
    • 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, 12208-12213 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12208-12213
    • Gallio, M.1    Sturgill, G.2    Rather, P.3    Kylsten, P.4
  • 56
    • 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, 1507-1512 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 1507-1512
    • Urban, S.1    Schlieper, D.2    Freeman, M.3
  • 58
    • 0027934803 scopus 로고
    • Characterization of aarA, a pleiotrophic negative regulator of the 2′-N-aceytransferase in Providencia stuartii
    • Rather, P. N. & Orosz, E. Characterization of aarA, a pleiotrophic negative regulator of the 2′-N-aceytransferase in Providencia stuartii. J. Bacteriol. 176, 5140-5144 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 5140-5144
    • Rather, P.N.1    Orosz, E.2
  • 59
    • 0032699221 scopus 로고    scopus 로고
    • Providencia stuartii genes activated by cell-to-cell signaling and identification of a gene required for production or activity of an extracellular factor
    • Rather, P. N., Ding, X., Baca-DeLancey, R. R. & Siddiqui, S. Providencia stuartii genes activated by cell-to-cell signaling and identification of a gene required for production or activity of an extracellular factor. J. Bactariol. 161, 7185-7191 (1999). References 55, 56 and 59 describe evidence that rhomboid from the bacterium Providencia stuartii controls the emission of a quorum-sensing signal. These papers provide the first evidence for shared mechanisms of intercellular signalling between bacteria and animals.
    • (1999) J. Bactariol. , vol.161 , pp. 7185-7191
    • Rather, P.N.1    Ding, X.2    Baca-DeLancey, R.R.3    Siddiqui, S.4
  • 60
    • 0034609723 scopus 로고    scopus 로고
    • Providencia may help find a function for a novel, widespread protein family
    • Gallio, M. & Kylsten, P. Providencia may help find a function for a novel, widespread protein family. Curr. Biol. 10, R693-R694 (2000).
    • (2000) Curr. Biol. , vol.10
    • Gallio, M.1    Kylsten, P.2
  • 61
    • 0036198860 scopus 로고    scopus 로고
    • Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae
    • Dimmer, K. S. et al. Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol. Biol. Cell 13, 847-853 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 847-853
    • Dimmer, K.S.1
  • 62
    • 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, 537-541 (2003).
    • (2003) Nature , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 63
    • 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, 27781-27788 (2003). References 62 and 63 show that a mitochondrial rhomboid in yeast controls mitochondrial membrane fusion by cleaving the dynamin-like GTPase Mgm1. Reference 62 also shows that mitochondrial rhomboids are conserved in humans and other eukaryotes.
    • (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
  • 64
    • 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, 835-843 (2002). The first report of proteolysis by a mitochondrial rhomboid in yeast. In this case the substrate was cytochrome-c peroxidase.
    • (2002) J. Mol. Biol. , vol.323 , pp. 835-843
    • Esser, K.1    Tursun, B.2    Ingenhoven, M.3    Michaelis, G.4    Pratje, E.5
  • 65
    • 0033593816 scopus 로고    scopus 로고
    • The yeast dynamin-like protein, Mgml p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance
    • Shepard, K. A. & Yaffe, M. P. The yeast dynamin-like protein, Mgml p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance. J. Cell Biol. 144, 711-720 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 711-720
    • Shepard, K.A.1    Yaffe, M.P.2
  • 66
    • 0034676095 scopus 로고    scopus 로고
    • The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mirochondria
    • Wong, E. D. et al. The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mirochondria. J. Cell Biol. 151, 341-352 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 341-352
    • Wong, E.D.1
  • 67
    • 0037415638 scopus 로고    scopus 로고
    • The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion
    • Wong, E. D. et al. The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion. J. Cell Biol. 160, 303-311 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 303-311
    • Wong, E.D.1
  • 68
    • 0043095416 scopus 로고    scopus 로고
    • Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnml p-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 Dnml p-dependent manner, but remain competent for mitochondrial fusion. Biochem. Biophys. Res. Commun. 308, 276-283 (2003).
    • (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
  • 69
    • 0033772264 scopus 로고    scopus 로고
    • OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
    • Alexander, C. et al. OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nature Genet. 26, 211-215 (2000).
    • (2000) Nature Genet. , vol.26 , pp. 211-215
    • Alexander, C.1
  • 70
    • 0036796861 scopus 로고    scopus 로고
    • Signaling from germ cells mediated by the rhomboid homolog stet organizes encapsulation by somatic support cells
    • Schulz, C., Wood, C. G., Jones, D. L., Tazuke, S. I. & Fuller, M. T Signaling from germ cells mediated by the rhomboid homolog stet organizes encapsulation by somatic support cells. Development 129, 4523-4534 (2002).
    • (2002) Development , vol.129 , pp. 4523-4534
    • Schulz, C.1    Wood, C.G.2    Jones, D.L.3    Tazuke, S.I.4    Fuller, M.T.5
  • 71
    • 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, 73-77 (2002).
    • (2002) Mech. Dev. , vol.113 , pp. 73-77
    • Jaszai, J.1    Brand, M.2
  • 72
    • 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, 337-340 (1998).
    • (1998) FEBS Lett. , vol.429 , pp. 337-340
    • Pascall, J.C.1    Brown, K.D.2
  • 73
    • 0037066757 scopus 로고    scopus 로고
    • Tumor necrosis factor-α converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability
    • Sunnarborg, S. W. et al. Tumor necrosis factor-α converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability. J Biol. Chem, 277, 12838-12845 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12838-12845
    • Sunnarborg, S.W.1
  • 74
    • 0037416187 scopus 로고    scopus 로고
    • TACE is required for the activation of the EGFR by TGF-α in tumors
    • Borrell-Pages, M., Rojo, F., Albanell, J., Baselga, J. & Arribas, J. TACE is required for the activation of the EGFR by TGF-α in tumors. EMBO J. 22, 1114-1124 (2003).
    • (2003) EMBO J. , vol.22 , pp. 1114-1124
    • Borrell-Pages, M.1    Rojo, F.2    Albanell, J.3    Baselga, J.4    Arribas, J.5
  • 75
    • 0032515018 scopus 로고    scopus 로고
    • An essential role for ectodomain shedding in mammalian development
    • Peschon, J. J. et al. An essential role for ectodomain shedding in mammalian development. Science 282, 1281-1284 (1998).
    • (1998) Science , vol.282 , pp. 1281-1284
    • Peschon, J.J.1
  • 77
    • 0014682668 scopus 로고
    • Structure of subtilisin BPN' at 2.5 angstrom resolution
    • Wright, C. S., Alden, R. A. & Kraut, J. Structure of subtilisin BPN' at 2.5 angstrom resolution. Nature 221, 235-242 (1969).
    • (1969) Nature , vol.221 , pp. 235-242
    • Wright, C.S.1    Alden, R.A.2    Kraut, J.3
  • 78
    • 0036777494 scopus 로고    scopus 로고
    • Intramembrane proteolysis controls diverse signaling pathways throughout evolution
    • Urban, S. & Freeman, M. Intramembrane proteolysis controls diverse signaling pathways throughout evolution. Curr. Opin. Genet. Dev. 12, 512-518 (2002).
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 512-518
    • Urban, S.1    Freeman, M.2
  • 79
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown, M. S., Ye, J., Rawson, R. B. & Goldstein, J. L. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100, 391-398 (2000). An influential and important review that first described the phenomenon of intramembrane proteolysis; it coined the much-used term RIP for regulated intramembrane proteolysis.
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 80
    • 0037304947 scopus 로고    scopus 로고
    • Intramembrane cleaving proteases: Controlled liberation of proteins and bioactive peptides
    • Weihofen, A. & Martoglio, B. Intramembrane cleaving proteases: controlled liberation of proteins and bioactive peptides. Trends Cell Biol. 13, 71-78 (2003).
    • (2003) Trends Cell Biol. , vol.13 , pp. 71-78
    • Weihofen, A.1    Martoglio, B.2
  • 81
    • 0035514568 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis takes another twist
    • Huppert, S. & Kopan, R. Regulated intramembrane proteolysis takes another twist. Dev. Cell 1, 590-592 (2001).
    • (2001) Dev. Cell , vol.1 , pp. 590-592
    • Huppert, S.1    Kopan, R.2
  • 82
    • 0028820299 scopus 로고
    • Hairpin orientation of sterol regulatory element-binding protein-2 in cell membranes as determined by protease protection
    • Hua, X., Sakai, J., Ho, Y. K., Goldstein, J. L. & Brown, M. S. Hairpin orientation of sterol regulatory element-binding protein-2 in cell membranes as determined by protease protection. J. Biol Chem. 270, 29422-29427 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 29422-29427
    • Hua, X.1    Sakai, J.2    Ho, Y.K.3    Goldstein, J.L.4    Brown, M.S.5
  • 83
    • 0032504202 scopus 로고    scopus 로고
    • Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning
    • Duncan, E. A., Dave, U. P., Sakai, J., Goldstein, J. L. & Brown, M. S. Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning. J. Biol. Chem. 273, 17801-17809 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 17801-17809
    • Duncan, E.A.1    Dave, U.P.2    Sakai, J.3    Goldstein, J.L.4    Brown, M.S.5
  • 84
    • 18444417998 scopus 로고    scopus 로고
    • Aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation
    • Francis, R. et al. aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation. Dev. Cell 3, 85-97 (2002).
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1
  • 85
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
    • Yu, G. et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 407, 48-54 (2000).
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1
  • 86
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and Nicastrin with Presenilin generate an active γ-Secretase complex
    • De Strooper, B. Aph-1, Pen-2, and Nicastrin with Presenilin generate an active γ-Secretase complex. Neuron 38, 9-12 (2003).
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 87
    • 0034613193 scopus 로고    scopus 로고
    • Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor
    • Weihofen, A., Lemberg, M. K., Ploegh, H. L., Bogyo, M. & Martoglio, B. Release of signal peptide fragments into the cytosol requires cleavage in the transmembrane region by a protease activity that is specifically blocked by a novel cysteine protease inhibitor. J. Biol. Chem. 275, 30951-30956 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 30951-30956
    • Weihofen, A.1    Lemberg, M.K.2    Ploegh, H.L.3    Bogyo, M.4    Martoglio, B.5
  • 88
    • 0038664363 scopus 로고    scopus 로고
    • Reconstitution of γ-secretase activity
    • Edbauer, D. et al. Reconstitution of γ-secretase activity. Nature Cell Biol. 5, 486-488 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 486-488
    • Edbauer, D.1
  • 89
    • 0035827339 scopus 로고    scopus 로고
    • A genomic perspective on human proteases
    • Southan, C. A genomic perspective on human proteases. FEBS Lett. 498, 214-218 (2001).
    • (2001) FEBS Lett. , vol.498 , pp. 214-218
    • Southan, C.1
  • 90
    • 0036551587 scopus 로고    scopus 로고
    • Secretase as a target for Alzheimer's disease
    • Wolfe, M. S. Secretase as a target for Alzheimer's disease. Curr Top. Med. Chem. 2, 371-383 (2002).
    • (2002) Curr. Top. Med. Chem. , vol.2 , pp. 371-383
    • Wolfe, M.S.1
  • 91
    • 0033599028 scopus 로고    scopus 로고
    • Transport-dependent proteolysis of SREBP: Relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
    • DeBose-Boyd, R. A. et al. Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi. Cell 99, 703-712 (1999).
    • (1999) Cell , vol.99 , pp. 703-712
    • DeBose-Boyd, R.A.1
  • 92
    • 0033613126 scopus 로고    scopus 로고
    • Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi
    • Nohturfft, A., DeBose-Boyd, R. A., Scheek, S., Goldstein, J. L. & Brown, M. S. Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi. Proc. Natl Acad. Sci. USA 96, 11235-11240 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11235-11240
    • Nohturfft, A.1    DeBose-Boyd, R.A.2    Scheek, S.3    Goldstein, J.L.4    Brown, M.S.5
  • 93
    • 0036792050 scopus 로고    scopus 로고
    • Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins
    • Yabe, D., Brown, M. S. & Goldstein, J. L. Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins. Proc. Natl Acad. Sci. USA 99, 12753-12758 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12753-12758
    • Yabe, D.1    Brown, M.S.2    Goldstein, J.L.3
  • 94
    • 0037162719 scopus 로고    scopus 로고
    • Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER
    • Yang, T. et al. Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 110, 489-500 (2002).
    • (2002) Cell , vol.110 , pp. 489-500
    • Yang, T.1
  • 95
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye, J. et al. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 6, 1355-1364 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1355-1364
    • Ye, J.1
  • 96
    • 0033593022 scopus 로고    scopus 로고
    • A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors
    • Rudner, D. Z., Fawcett, P. & Losick, R. A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors. Proc. Natl Acad. Sci. USA 96, 14765-14770 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14765-14770
    • Rudner, D.Z.1    Fawcett, P.2    Losick, R.3
  • 97
    • 0032871073 scopus 로고    scopus 로고
    • Identification and characterization of a determinant (eep) on the Enterococcus faecalis chromosome that is involved in production of the peptide sex pheromone cAD1
    • An, F. Y., Sulavik, M. C. & Clewell, D. B, Identification and characterization of a determinant (eep) on the Enterococcus faecalis chromosome that is involved in production of the peptide sex pheromone cAD1. J. Bacteriol. 161, 5915-5921 (1999).
    • (1999) J. Bacteriol. , vol.161 , pp. 5915-5921
    • An, F.Y.1    Sulavik, M.C.2    Clewell, D.B.3
  • 98
    • 0036211978 scopus 로고    scopus 로고
    • Identification of the cAD1 sex pheromone precursor in Enterococcus faecalis
    • An, F. Y. & Clewell, D. B. Identification of the cAD1 sex pheromone precursor in Enterococcus faecalis. J. Bacteriol. 184, 1880-1887 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 1880-1887
    • An, F.Y.1    Clewell, D.B.2
  • 99
    • 0029115555 scopus 로고
    • The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families
    • Alzheimer's Disease Collaborative Group. The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families. Nature Genet. 11, 219-222 (1995).
    • (1995) Nature Genet. , vol.11 , pp. 219-222
  • 100
    • 0036855661 scopus 로고    scopus 로고
    • Deciphering the genesis and fate of amyloid β-protein yields novel therapies for Alzheimer disease
    • Selkoe, D. J. Deciphering the genesis and fate of amyloid β-protein yields novel therapies for Alzheimer disease. J. Clin. Invest. 110, 1375-1381 (2002).
    • (2002) J. Clin. Invest. , vol.110 , pp. 1375-1381
    • Selkoe, D.J.1
  • 101
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
    • De Strooper, B. et al. A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain. Nature 398, 518-522 (1999).
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1
  • 102
    • 0033535508 scopus 로고    scopus 로고
    • Presenilin is required for activity and nuclear access of Notch in Drosophila
    • Struhl, G. & Greenwald, I. Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature 398, 522-525 (1999).
    • (1999) Nature , vol.398 , pp. 522-525
    • Struhl, G.1    Greenwald, I.2
  • 103
    • 0032524325 scopus 로고    scopus 로고
    • Nuclear access and action of notch in vivo
    • Struhl, G. & Adachi, A. Nuclear access and action of notch in vivo. Cell 93, 649-660 (1998).
    • (1998) Cell , vol.93 , pp. 649-660
    • Struhl, G.1    Adachi, A.2
  • 104
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter, E. H., Kisslinger, J. A. & Kopan, R. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393, 382-386 (1998).
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 105
    • 0032543565 scopus 로고    scopus 로고
    • Indirect evidence for Delta-dependent intracellular processing of notch in Drosophila embryos
    • Lecourtois, M. & Schweisguth, F. Indirect evidence for Delta-dependent intracellular processing of notch in Drosophila embryos. Curr. Biol. 8, 771-774 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 771-774
    • Lecourtois, M.1    Schweisguth, F.2
  • 106
    • 0141994826 scopus 로고    scopus 로고
    • Intramembrane-cleaving aspartic proteases and disease: Presenilins, signal peptide peptidase and their homologs
    • Martoglio, B, & Golde, T E. Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs. Hum. Mol. Genet. 12 (Suppl. 2), R201-R206 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , Issue.SUPPL. 2
    • Martoglio, B.1    Golde, T.E.2
  • 107
    • 0036683052 scopus 로고    scopus 로고
    • Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets
    • McLauchlan, J., Lemberg, M. K., Hope, G, & Martoglio, B. Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets. EMBO J. 21, 3980-3988 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3980-3988
    • McLauchlan, J.1    Lemberg, M.K.2    Hope, G.3    Martoglio, B.4


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