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Volumn 1828, Issue 12, 2013, Pages 2862-2872

Untangling structure-function relationships in the rhomboid family of intramembrane proteases

Author keywords

GlpG; Intramembrane protease; Membrane protein structure; Rhomboid protease; Serine protease; X ray crystallography

Indexed keywords

BACTERIAL ENZYME; GLPG PROTEIN; MEMBRANE PROTEIN; RHOMBOID PROTEIN; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 84885161299     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.05.003     Document Type: Review
Times cited : (23)

References (71)
  • 1
    • 63649142567 scopus 로고    scopus 로고
    • Rhomboids: 7 years of a new protease family
    • M. Freeman Rhomboids: 7 years of a new protease family Semin. Cell Dev. Biol. 20 2009 231 239
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 231-239
    • Freeman, M.1
  • 2
    • 80054893675 scopus 로고    scopus 로고
    • The rhomboid protease family: A decade of progress on function and mechanism
    • S. Urban, and S.W. Dickey The rhomboid protease family: a decade of progress on function and mechanism Genome Biol. 12 2011 231
    • (2011) Genome Biol. , vol.12 , pp. 231
    • Urban, S.1    Dickey, S.W.2
  • 3
    • 0024114027 scopus 로고
    • A group of genes required for pattern formation in the ventral ectoderm of the Drosophila embryo
    • U. Mayer, and C. Nusslein-Volhard A group of genes required for pattern formation in the ventral ectoderm of the Drosophila embryo Genes Dev. 2 1988 1496 1511
    • (1988) Genes Dev. , vol.2 , pp. 1496-1511
    • Mayer, U.1    Nusslein-Volhard, C.2
  • 4
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila Rhomboid-1 defines a family of putative intramembrane serine proteases
    • DOI 10.1016/S0092-8674(01)00525-6
    • S. Urban, J.R. Lee, and M. Freeman Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases Cell 107 2001 173 182 (Pubitemid 33035944)
    • (2001) Cell , vol.107 , Issue.2 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 5
    • 0037264371 scopus 로고    scopus 로고
    • The rhomboids: A nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers
    • E.V. Koonin, K.S. Makarova, I.B. Rogozin, L. Davidovic, M.C. Letellier, and L. Pellegrini 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
  • 6
    • 67349117281 scopus 로고    scopus 로고
    • Making the cut: Central roles of intramembrane proteolysis in pathogenic microorganisms
    • S. Urban Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms Nat. Rev. Microbiol. 7 2009 411 423
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 411-423
    • Urban, S.1
  • 7
    • 58549108805 scopus 로고    scopus 로고
    • Rhomboid proteases and their biological functions
    • M. Freeman Rhomboid proteases and their biological functions Annu. Rev. Genet. 42 2008 191 210
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 191-210
    • Freeman, M.1
  • 8
    • 35948982252 scopus 로고    scopus 로고
    • Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases
    • DOI 10.1101/gr.6425307
    • M.K. Lemberg, and M. Freeman Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases Genome Res. 17 2007 1634 1646 (Pubitemid 350074859)
    • (2007) Genome Research , vol.17 , Issue.11 , pp. 1634-1646
    • Lemberg, M.K.1    Freeman, M.2
  • 9
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Y. Wang, Y. Zhang, and Y. Ha Crystal structure of a rhomboid family intramembrane protease Nature 444 2006 179 180
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 13
    • 35748974498 scopus 로고    scopus 로고
    • The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG
    • DOI 10.1016/j.jmb.2007.10.014, PII S0022283607013356
    • Y. Wang, S. Maegawa, Y. Akiyama, and Y. Ha The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG J. Mol. Biol. 374 2007 1104 1113 (Pubitemid 350052106)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.4 , pp. 1104-1113
    • Wang, Y.1    Maegawa, S.2    Akiyama, Y.3    Ha, Y.4
  • 15
    • 79952316125 scopus 로고    scopus 로고
    • Structure of rhomboid protease in a lipid environment
    • K.R. Vinothkumar Structure of rhomboid protease in a lipid environment J. Mol. Biol. 407 2011 232 247
    • (2011) J. Mol. Biol. , vol.407 , pp. 232-247
    • Vinothkumar, K.R.1
  • 16
    • 84856292019 scopus 로고    scopus 로고
    • Catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate
    • Y. Xue, and Y. Ha Catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate J. Biol. Chem. 287 2012 3099 3107
    • (2012) J. Biol. Chem. , vol.287 , pp. 3099-3107
    • Xue, Y.1    Ha, Y.2
  • 17
    • 84860711067 scopus 로고    scopus 로고
    • Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S′ subsites
    • Y. Xue, S. Chowdhury, X. Liu, Y. Akiyama, J. Ellman, and Y. Ha Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S′ subsites Biochemistry 51 2012 3723 3731
    • (2012) Biochemistry , vol.51 , pp. 3723-3731
    • Xue, Y.1    Chowdhury, S.2    Liu, X.3    Akiyama, Y.4    Ellman, J.5    Ha, Y.6
  • 21
    • 74349127184 scopus 로고    scopus 로고
    • Taking the plunge: Integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis
    • S. Urban Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis Biochem. J. 425 2010 501 512
    • (2010) Biochem. J. , vol.425 , pp. 501-512
    • Urban, S.1
  • 23
    • 33751436135 scopus 로고    scopus 로고
    • Solution Structure and Dynamics of the N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Pseudomonas aeruginosa: Insights into a Functional Role in Intramembrane Proteolysis
    • DOI 10.1016/j.jmb.2006.09.047, PII S0022283606012563
    • A. Del Rio, K. Dutta, J. Chavez, I. Ubarretxena-Belandia, and R. Ghose Solution structure and dynamics of the N-terminal cytosolic domain of rhomboid intramembrane protease from Pseudomonas aeruginosa: insights into a functional role in intramembrane proteolysis J. Mol. Biol. 365 2007 109 122 (Pubitemid 44821200)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.1 , pp. 109-122
    • Del Rio, A.1    Dutta, K.2    Chavez, J.3    Ubarretxena-Belandia, I.4    Ghose, R.5
  • 24
    • 84867073516 scopus 로고    scopus 로고
    • Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core
    • A.R. Sherratt, D.R. Blais, H. Ghasriani, J.P. Pezacki, and N.K. Goto Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core Biochemistry 51 2012 7794 7803
    • (2012) Biochemistry , vol.51 , pp. 7794-7803
    • Sherratt, A.R.1    Blais, D.R.2    Ghasriani, H.3    Pezacki, J.P.4    Goto, N.K.5
  • 25
    • 84875223117 scopus 로고    scopus 로고
    • Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease
    • C. Lazareno-Saez, E. Arutyunova, N. Coquelle, and M.J. Lemieux Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease J. Mol. Biol. 425 2013 1127 1142
    • (2013) J. Mol. Biol. , vol.425 , pp. 1127-1142
    • Lazareno-Saez, C.1    Arutyunova, E.2    Coquelle, N.3    Lemieux, M.J.4
  • 26
    • 0030759097 scopus 로고    scopus 로고
    • The tortuous story of Asp...His...Ser: Structural analysis of alpha-chymotrypsin
    • DOI 10.1016/S0968-0004(97)01115-8, PII S0968000497011158
    • D.M. Blow The tortuous story of Asp. His. Ser: structural analysis of alpha-chymotrypsin Trends Biochem. Sci. 22 1997 405 408 (Pubitemid 27438205)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.10 , pp. 405-408
    • Blow, D.M.1
  • 27
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • L. Hedstrom Serine protease mechanism and specificity Chem. Rev. 102 2002 4501 4524
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 28
    • 0033967856 scopus 로고    scopus 로고
    • MEROPS: The peptidase database
    • N.D. Rawlings, and A.J. Barrett MEROPS: the peptidase database Nucleic Acids Res. 28 2000 323 325 (Pubitemid 30047794)
    • (2000) Nucleic Acids Research , vol.28 , Issue.1 , pp. 323-325
    • Rawlings, N.D.1    Barrett, A.J.2
  • 29
    • 0001109389 scopus 로고
    • Stereochemistry of reaction paths at carbonyl centers
    • H.B. Burgi, J.D. Dunitz, J.M. Lehn, and G. Wipff Stereochemistry of reaction paths at carbonyl centers Tetrahedron 30 1974 1563 1572
    • (1974) Tetrahedron , vol.30 , pp. 1563-1572
    • Burgi, H.B.1    Dunitz, J.D.2    Lehn, J.M.3    Wipff, G.4
  • 30
    • 84864684042 scopus 로고    scopus 로고
    • Importance of tetrahedral intermediate formation in the catalytic mechanism of the serine proteases chymotrypsin and subtilisin
    • T. Petrillo, C.A. O'Donohoe, N. Howe, and J.P.G. Malthouse Importance of tetrahedral intermediate formation in the catalytic mechanism of the serine proteases chymotrypsin and subtilisin Biochemistry 51 2012 6164 6170
    • (2012) Biochemistry , vol.51 , pp. 6164-6170
    • Petrillo, T.1    O'Donohoe, C.A.2    Howe, N.3    Malthouse, J.P.G.4
  • 31
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta- lactam inhibitor
    • DOI 10.1038/24196
    • M. Paetzel, R.E. Dalbey, and N.C.J. Strynadka Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor Nature 396 1998 186 190 (Pubitemid 28523623)
    • (1998) Nature , vol.396 , Issue.6707 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.J.3
  • 32
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • J.C. Powers, J.L. Asgian, O.D. Ekici, and K.E. James Irreversible inhibitors of serine, cysteine, and threonine proteases Chem. Rev. 102 2002 4639 4750
    • (2002) Chem. Rev. , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 33
    • 13844306483 scopus 로고    scopus 로고
    • Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity
    • DOI 10.1073/pnas.0408306102
    • S. Urban, and M.S. Wolfe Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity Proc. Natl. Acad. Sci. U. S. A. 102 2005 1883 1888 (Pubitemid 40261981)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.6 , pp. 1883-1888
    • Urban, S.1    Wolfe, M.S.2
  • 37
    • 50849109498 scopus 로고    scopus 로고
    • In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells
    • S. Urban, and R.P. Baker In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells Biol. Chem. 389 2008 1107 1115
    • (2008) Biol. Chem. , vol.389 , pp. 1107-1115
    • Urban, S.1    Baker, R.P.2
  • 38
    • 84863534125 scopus 로고    scopus 로고
    • An internal water-retention site in the rhomboid intramembrane protease GlpG ensures catalytic efficiency
    • Y. Zhou, S.M. Moin, S. Urban, and Y. Zhang An internal water-retention site in the rhomboid intramembrane protease GlpG ensures catalytic efficiency Structure 20 2012 1255 1263
    • (2012) Structure , vol.20 , pp. 1255-1263
    • Zhou, Y.1    Moin, S.M.2    Urban, S.3    Zhang, Y.4
  • 39
    • 84865328335 scopus 로고    scopus 로고
    • Architectural and thermodynamic principles underlying intramembrane protease function
    • R.P. Baker, and S. Urban Architectural and thermodynamic principles underlying intramembrane protease function Nat. Chem. Biol. 8 2012 759 768
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 759-768
    • Baker, R.P.1    Urban, S.2
  • 40
    • 84878843045 scopus 로고    scopus 로고
    • Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics
    • S.M. Moin, and S. Urban Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics eLife 1 2012 e00173
    • (2012) ELife , vol.1 , pp. 00173
    • Moin, S.M.1    Urban, S.2
  • 41
    • 84865156638 scopus 로고    scopus 로고
    • Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes
    • M.J. Fritsch, M. Krehenbrink, M.J. Tarry, B.C. Berks, and T. Palmer Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes Mol. Microbiol. 84 2012 1108 1123
    • (2012) Mol. Microbiol. , vol.84 , pp. 1108-1123
    • Fritsch, M.J.1    Krehenbrink, M.2    Tarry, M.J.3    Berks, B.C.4    Palmer, T.5
  • 43
    • 0037126036 scopus 로고    scopus 로고
    • A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes
    • M. Gallio, G. Sturgill, P. Rather, and P. Kylsten A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes Proc. Natl. Acad. Sci. U. S. A. 99 2002 12208 12213
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12208-12213
    • Gallio, M.1    Sturgill, G.2    Rather, P.3    Kylsten, P.4
  • 44
    • 33646255954 scopus 로고    scopus 로고
    • Functional characterization of Escherichia coli GlpG and additional rhomboid proteins using an aarA mutant of Providencia stuartii
    • K.M. Clemmer, G.M. Sturgill, A. Veenstra, and P.N. Rather Functional characterization of Escherichia coli GlpG and additional rhomboid proteins using an aarA mutant of Providencia stuartii J. Bacteriol. 188 2006 3415 3419
    • (2006) J. Bacteriol. , vol.188 , pp. 3415-3419
    • Clemmer, K.M.1    Sturgill, G.M.2    Veenstra, A.3    Rather, P.N.4
  • 46
    • 0037015265 scopus 로고    scopus 로고
    • Conservation of intramembrane proteolytic activity and substrate specificity in prokaryotic and eukaryotic rhomboids
    • DOI 10.1016/S0960-9822(02)01092-8, PII S0960982202010928
    • S. Urban, D. Schlieper, and M. Freeman Conservation of intramembrane proteolytic activity and substrate specificity in prokaryotic and eukaryotic rhomboids Curr. Biol. 12 2002 1507 1512 (Pubitemid 35036649)
    • (2002) Current Biology , vol.12 , Issue.17 , pp. 1507-1512
    • Urban, S.1    Schlieper, D.2    Freeman, M.3
  • 48
    • 0038771224 scopus 로고    scopus 로고
    • Substrate specificity of Rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain
    • DOI 10.1016/S1097-2765(03)00181-3
    • S. Urban, and M. Freeman Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain Mol. Cell 11 2003 1425 1434 (Pubitemid 36776530)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 49
    • 34248371981 scopus 로고    scopus 로고
    • Sequence features of substrates required for cleavage by GlpG, an Escherichia coli rhomboid protease
    • DOI 10.1111/j.1365-2958.2007.05715.x
    • Y. Akiyama, and S. Maegawa Sequence features of substrates required for cleavage by GlpG, an Escherichia coli rhomboid protease Mol. Microbiol. 64 2007 1028 1037 (Pubitemid 46743969)
    • (2007) Molecular Microbiology , vol.64 , Issue.4 , pp. 1028-1037
    • Akiyama, Y.1    Maegawa, S.2
  • 50
    • 72149124813 scopus 로고    scopus 로고
    • Sequence-specific intramembrane proteolysis: Identification of a recognition motif in rhomboid substrates
    • K. Strisovsky, H.J. Sharpe, and M. Freeman Sequence-specific intramembrane proteolysis: identification of a recognition motif in rhomboid substrates Mol. Cell 36 2009 1048 1059
    • (2009) Mol. Cell , vol.36 , pp. 1048-1059
    • Strisovsky, K.1    Sharpe, H.J.2    Freeman, M.3
  • 51
    • 77955085749 scopus 로고    scopus 로고
    • Intramembrane proteolysis of Mgm1 by the mitochondrial rhomboid protease is highly promiscuous regarding the sequence of the cleaved hydrophobic segment
    • A. Schafer, M. Zick, J. Kief, M. Steger, H. Heide, S. Duvezin-Caubet, W. Neupert, and A.S. Reichert Intramembrane proteolysis of Mgm1 by the mitochondrial rhomboid protease is highly promiscuous regarding the sequence of the cleaved hydrophobic segment J. Mol. Biol. 401 2010 182 193
    • (2010) J. Mol. Biol. , vol.401 , pp. 182-193
    • Schafer, A.1    Zick, M.2    Kief, J.3    Steger, M.4    Heide, H.5    Duvezin-Caubet, S.6    Neupert, W.7    Reichert, A.S.8
  • 52
    • 84864751064 scopus 로고    scopus 로고
    • Multifaceted substrate capture scheme of a rhomboid protease
    • T. Reddy, and J.K. Rainey Multifaceted substrate capture scheme of a rhomboid protease J. Phys. Chem. C 116 2012 8942 8954
    • (2012) J. Phys. Chem. C , vol.116 , pp. 8942-8954
    • Reddy, T.1    Rainey, J.K.2
  • 53
    • 26644441432 scopus 로고    scopus 로고
    • Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane
    • DOI 10.1021/bi051363k
    • S. Maegawa, K. Ito, and Y. Akiyama Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane Biochemistry 44 2005 13543 13552 (Pubitemid 41443681)
    • (2005) Biochemistry , vol.44 , Issue.41 , pp. 13543-13552
    • Maegawa, S.1    Ito, K.2    Akiyama, Y.3
  • 55
    • 61549125968 scopus 로고    scopus 로고
    • Rhomboid protease dynamics and lipid interactions
    • A.N. Bondar, C. del Val, and S.H. White Rhomboid protease dynamics and lipid interactions Structure 17 2009 395 405
    • (2009) Structure , vol.17 , pp. 395-405
    • Bondar, A.N.1    Del Val, C.2    White, S.H.3
  • 56
    • 84857933257 scopus 로고    scopus 로고
    • Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module
    • N. Zeytuni, and R. Zarivach Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module Structure 20 2012 397 405
    • (2012) Structure , vol.20 , pp. 397-405
    • Zeytuni, N.1    Zarivach, R.2
  • 57
    • 33748630199 scopus 로고    scopus 로고
    • Cross genome comparisons of serine proteases in Arabidopsis and rice
    • L.P. Tripathi, and R. Sowdhamini Cross genome comparisons of serine proteases in Arabidopsis and rice BMC Genomics 7 2006 200
    • (2006) BMC Genomics , vol.7 , pp. 200
    • Tripathi, L.P.1    Sowdhamini, R.2
  • 58
    • 33750555919 scopus 로고    scopus 로고
    • Ubiquitin-binding domains
    • DOI 10.1042/BJ20061138
    • J.H. Hurley, S. Lee, and G. Prag Ubiquitin-binding domains Biochem. J. 399 2006 361 372 (Pubitemid 44672627)
    • (2006) Biochemical Journal , vol.399 , Issue.3 , pp. 361-372
    • Hurley, J.H.1    Lee, S.2    Prag, G.3
  • 59
    • 0036339998 scopus 로고    scopus 로고
    • Mechanism of activation of the Drosophila EGF receptor by the TGFalpha ligand gurken during oogenesis
    • C. Ghiglione, E.A. Bach, Y. Paraiso, K.L. Carraway III, S. Noselli, and N. Perrimon Mechanism of activation of the Drosophila EGF receptor by the TGFalpha ligand Gurken during oogenesis Development 129 2002 175 186 (Pubitemid 34863786)
    • (2002) Development , vol.129 , Issue.1 , pp. 175-186
    • Ghiglione, C.1    Bach, E.A.2    Paraiso, Y.3    Carraway III, K.L.4    Noselli, S.5    Perrimon, N.6
  • 60
    • 0035913906 scopus 로고    scopus 로고
    • Regulated intracellular ligand transport and proteolysis control EGF signal activation in Drosophila
    • DOI 10.1016/S0092-8674(01)00526-8
    • J.R. Lee, S. Urban, C.F. Garvey, and M. Freeman Regulated intracellular ligand transport and proteolysis control EGF signal activation in Drosophila Cell 107 2001 161 171 (Pubitemid 33035943)
    • (2001) Cell , vol.107 , Issue.2 , pp. 161-171
    • Lee, J.R.1    Urban, S.2    Garvey, C.F.3    Freeman, M.4
  • 61
    • 0037080869 scopus 로고    scopus 로고
    • Intracellular trafficking by Star regulates cleavage of the Drosophila EGF receptor ligand Spitz
    • DOI 10.1101/gad.214202
    • R. Tsruya, A. Schlesinger, A. Reich, L. Gabay, A. Sapir, and B.Z. Shilo Intracellular trafficking by Star regulates cleavage of the Drosophila EGF receptor ligand Spitz Genes Dev. 16 2002 222 234 (Pubitemid 34075814)
    • (2002) Genes and Development , vol.16 , Issue.2 , pp. 222-234
    • Tsruya, R.1    Schlesinger, A.2    Reich, A.3    Gabay, L.4    Sapir, A.5    Shilo, B.-Z.6
  • 62
    • 42449109164 scopus 로고    scopus 로고
    • Drosophila EGFR signalling is modulated by differential compartmentalization of Rhomboid intramembrane proteases
    • DOI 10.1038/emboj.2008.58, PII EMBOJ200858
    • S. Yogev, E.D. Schejter, and B.Z. Shilo Drosophila EGFR signalling is modulated by differential compartmentalization of rhomboid intramembrane proteases EMBO J. 27 2008 1219 1230 (Pubitemid 351574753)
    • (2008) EMBO Journal , vol.27 , Issue.8 , pp. 1219-1230
    • Yogev, S.1    Schejter, E.D.2    Shilo, B.-Z.3
  • 63
    • 41849117736 scopus 로고    scopus 로고
    • Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii
    • DOI 10.1111/j.1600-0854.2008.00736.x
    • L. Sheiner, T.J. Dowse, and D. Soldati-Favre Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii Traffic 9 2008 665 677 (Pubitemid 351494299)
    • (2008) Traffic , vol.9 , Issue.5 , pp. 665-677
    • Sheiner, L.1    Dowse, T.J.2    Soldati-Favre, D.3
  • 64
    • 84865389259 scopus 로고    scopus 로고
    • Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins
    • L. Fleig, N. Bergbold, P. Sahasrabudhe, B. Geiger, L. Kaltak, and M.K. Lemberg Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins Mol. Cell 47 2012 558 569
    • (2012) Mol. Cell , vol.47 , pp. 558-569
    • Fleig, L.1    Bergbold, N.2    Sahasrabudhe, P.3    Geiger, B.4    Kaltak, L.5    Lemberg, M.K.6
  • 65
    • 1242288387 scopus 로고    scopus 로고
    • Diverse substrate recognition mechanisms for rhomboids: Thrombomodulin is cleaved by mammalian rhomboids
    • DOI 10.1016/S0960-9822(04)00008-9
    • O. Lohi, S. Urban, and M. Freeman Diverse substrate recognition mechanisms for rhomboids; thrombomodulin is cleaved by mammalian rhomboids Curr. Biol. CB 14 2004 236 241 (Pubitemid 38215352)
    • (2004) Current Biology , vol.14 , Issue.3 , pp. 236-241
    • Lohi, O.1    Urban, S.2    Freeman, M.3
  • 66
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • DOI 10.1016/j.jmb.2004.02.002, PII S0022283604001482
    • J.J. Ward, J.S. Sodhi, L.J. McGuffin, B.F. Buxton, and D.T. Jones Prediction and functional analysis of native disorder in proteins from the three kingdoms of life J. Mol. Biol. 337 2004 635 645 (Pubitemid 38326883)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.3 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 68
    • 0035369556 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems
    • DOI 10.1016/S0968-0004(01)01835-7, PII S0968000401018357
    • K. Hofmann, and L. Falquet A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems Trends Biochem. Sci. 26 2001 347 350 (Pubitemid 32530646)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.6 , pp. 347-350
    • Hofmann, K.1    Falquet, L.2
  • 70
    • 71149098713 scopus 로고    scopus 로고
    • Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain
    • A.R. Sherratt, M.V. Braganza, E. Nguyen, T. Ducat, and N.K. Goto Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain Biochim. Biophys. Acta 1788 2009 2444 2453
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2444-2453
    • Sherratt, A.R.1    Braganza, M.V.2    Nguyen, E.3    Ducat, T.4    Goto, N.K.5


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