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Volumn 110, Issue 7, 2013, Pages 2472-2477

Activity-based probes for rhomboid proteases discovered in a mass spectrometry-based assay

Author keywords

Covalent inhibition; MALDI screening; Regulated intramembrane proteolysis

Indexed keywords

PROTEINASE; RHOMBOID PROTEASE; SERINE; UNCLASSIFIED DRUG;

EID: 84873742188     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1215076110     Document Type: Article
Times cited : (55)

References (43)
  • 1
    • 84859366447 scopus 로고    scopus 로고
    • Protease signalling: The cutting edge
    • Turk B, Turk SA, Turk V (2012) Protease signalling: The cutting edge. EMBO J 31(7):1630-1643.
    • (2012) EMBO J , vol.31 , Issue.7 , pp. 1630-1643
    • Turk, B.1    Turk, S.A.2    Turk, V.3
  • 2
    • 79251491023 scopus 로고    scopus 로고
    • Current strategies for probing substrate specificity of proteases
    • Poreba M, Drag M (2010) Current strategies for probing substrate specificity of proteases. Curr Med Chem 17(33):3968-3995.
    • (2010) Curr Med Chem , vol.17 , Issue.33 , pp. 3968-3995
    • Poreba, M.1    Drag, M.2
  • 3
    • 84855428544 scopus 로고    scopus 로고
    • New approaches for dissecting protease functions to improve probe development and drug discovery
    • Deu E, Verdoes M, Bogyo M (2012) New approaches for dissecting protease functions to improve probe development and drug discovery. Nat Struct Mol Biol 19(1):9-16.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.1 , pp. 9-16
    • Deu, E.1    Verdoes, M.2    Bogyo, M.3
  • 4
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • Cravatt BF, Wright AT, Kozarich JW (2008) Activity-based protein profiling: From enzyme chemistry to proteomic chemistry. Annu Rev Biochem 77:383-414.
    • (2008) Annu Rev Biochem , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 5
    • 84862873324 scopus 로고    scopus 로고
    • Activity-based probes for the study of proteases: Recent advances and developments
    • Serim S, Haedke U, Verhelst SHL (2012) Activity-based probes for the study of proteases: Recent advances and developments. ChemMedChem 7(7):1146-1159.
    • (2012) ChemMedChem , vol.7 , Issue.7 , pp. 1146-1159
    • Serim, S.1    Haedke, U.2    Verhelst, S.H.L.3
  • 6
    • 74349127184 scopus 로고    scopus 로고
    • Taking the plunge: Integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis
    • Urban S (2010) Taking the plunge: Integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis. Biochem J 425(3):501-512.
    • (2010) Biochem J , vol.425 , Issue.3 , pp. 501-512
    • Urban, S.1
  • 7
    • 66249133368 scopus 로고    scopus 로고
    • How intramembrane proteases bury hydrolytic reactions in the membrane
    • Erez E, Fass D, Bibi E (2009) How intramembrane proteases bury hydrolytic reactions in the membrane. Nature 459(7245):371-378.
    • (2009) Nature , vol.459 , Issue.7245 , pp. 371-378
    • Erez, E.1    Fass, D.2    Bibi, E.3
  • 8
    • 65249188697 scopus 로고    scopus 로고
    • Intramembrane proteolysis
    • Wolfe MS (2009) Intramembrane proteolysis. Chem Rev 109(4):1599-1612.
    • (2009) Chem Rev , vol.109 , Issue.4 , pp. 1599-1612
    • Wolfe, M.S.1
  • 10
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila Rhomboid-1 defines a family of putative intramembrane serine proteases
    • DOI 10.1016/S0092-8674(01)00525-6
    • Urban S, Lee JR, Freeman M (2001) Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases. Cell 107(2):173-182. (Pubitemid 33035944)
    • (2001) Cell , vol.107 , Issue.2 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 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 EV, et al. (2003) The rhomboids: A nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers. Genome Biol 4(3):R19.
    • (2003) Genome Biol , vol.4 , Issue.3
    • Koonin, E.V.1
  • 12
    • 35948982252 scopus 로고    scopus 로고
    • Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases
    • DOI 10.1101/gr.6425307
    • Lemberg MK, Freeman M (2007) Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases. Genome Res 17(11):1634-1646. (Pubitemid 350074859)
    • (2007) Genome Research , vol.17 , Issue.11 , pp. 1634-1646
    • Lemberg, M.K.1    Freeman, M.2
  • 14
    • 33750465167 scopus 로고    scopus 로고
    • Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria
    • Baker RP, Wijetilaka R, Urban S (2006) Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria. PLoS Pathog 2(10):e113.
    • (2006) PLoS Pathog , vol.2 , Issue.10
    • Baker, R.P.1    Wijetilaka, R.2    Urban, S.3
  • 15
    • 33749342018 scopus 로고    scopus 로고
    • Intramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasite
    • O'Donnell RA, et al. (2006) Intramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasite. J Cell Biol 174(7):1023-1033.
    • (2006) J Cell Biol , vol.174 , Issue.7 , pp. 1023-1033
    • O'Donnell, R.A.1
  • 16
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Wang Y, Zhang Y, Ha Y (2006) Crystal structure of a rhomboid family intramembrane protease. Nature 444(7116):179-180.
    • (2006) Nature , vol.444 , Issue.7116 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 20
    • 70449642213 scopus 로고    scopus 로고
    • The processing of human rhomboid intramembrane serine protease RHBDL2 is required for its proteolytic activity
    • Lei X, Li YM (2009) The processing of human rhomboid intramembrane serine protease RHBDL2 is required for its proteolytic activity. J Mol Biol 394(5):815-825.
    • (2009) J Mol Biol , vol.394 , Issue.5 , pp. 815-825
    • Lei, X.1    Li, Y.M.2
  • 21
    • 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
    • Urban S, Wolfe MS (2005) Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity. Proc Natl Acad Sci USA 102(6):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
  • 22
    • 14844300797 scopus 로고    scopus 로고
    • Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases
    • DOI 10.1038/sj.emboj.7600537
    • Lemberg MK, et al. (2005) Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases. EMBO J 24(3):464-472. (Pubitemid 40343249)
    • (2005) EMBO Journal , vol.24 , Issue.3 , pp. 464-472
    • Lemberg, M.K.1    Menendez, J.2    Misik, A.3    Garcia, M.4    Koth, C.M.5    Freeman, M.6
  • 23
    • 78449268297 scopus 로고    scopus 로고
    • The structural basis for catalysis and substrate specificity of a rhomboid protease
    • Vinothkumar KR, et al. (2010) The structural basis for catalysis and substrate specificity of a rhomboid protease. EMBO J 29(22):3797-3809.
    • (2010) EMBO J , vol.29 , Issue.22 , pp. 3797-3809
    • Vinothkumar, K.R.1
  • 24
    • 79954613090 scopus 로고    scopus 로고
    • Monocyclic β-lactams are selective, mechanism-based inhibitors of rhomboid intramembrane proteases
    • Pierrat OA, et al. (2011) Monocyclic β-lactams are selective, mechanism-based inhibitors of rhomboid intramembrane proteases. ACS Chem Biol 6(4):325-335.
    • (2011) ACS Chem Biol , vol.6 , Issue.4 , pp. 325-335
    • Pierrat, O.A.1
  • 25
    • 84860711067 scopus 로고    scopus 로고
    • Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S′ subsites
    • Xue Y, et al. (2012) Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S′ subsites. Biochemistry 51(18):3723-3731.
    • (2012) Biochemistry , vol.51 , Issue.18 , pp. 3723-3731
    • Xue, Y.1
  • 26
    • 84867073516 scopus 로고    scopus 로고
    • Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core
    • Sherratt AR, Blais DR, Ghasriani H, Pezacki JP, Goto NK (2012) Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core. Biochemistry 51(39):7794-7803.
    • (2012) Biochemistry , vol.51 , Issue.39 , pp. 7794-7803
    • Sherratt, A.R.1    Blais, D.R.2    Ghasriani, H.3    Pezacki, J.P.4    Goto, N.K.5
  • 27
    • 26644441432 scopus 로고    scopus 로고
    • Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane
    • DOI 10.1021/bi051363k
    • Maegawa S, Ito K, Akiyama Y (2005) Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane. Biochemistry 44(41):13543-13552. (Pubitemid 41443681)
    • (2005) Biochemistry , vol.44 , Issue.41 , pp. 13543-13552
    • Maegawa, S.1    Ito, K.2    Akiyama, Y.3
  • 28
    • 3042587661 scopus 로고    scopus 로고
    • Increased peptide deformylase activity for N-formylmethionine processing of proteins overexpressed in Escherichia coli: Application to homogeneous rubredoxin production
    • DOI 10.1016/j.pep.2004.03.007, PII S1046592804001044
    • Tang J, Hernández G, LeMaster DM (2004) Increased peptide deformylase activity for N-formylmethionine processing of proteins overexpressed in Escherichia coli: Application to homogeneous rubredoxin production. Protein Expr Purif 36(1):100-105. (Pubitemid 38836770)
    • (2004) Protein Expression and Purification , vol.36 , Issue.1 , pp. 100-105
    • Tang, J.1    Hernandez, G.2    LeMaster, D.M.3
  • 29
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • DOI 10.1177/108705719900400206
    • Zhang JH, Chung TD, Oldenburg KR (1999) A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J Biomol Screen 4(2):67-73. (Pubitemid 29278954)
    • (1999) Journal of Biomolecular Screening , vol.4 , Issue.2 , pp. 67-73
    • Zhang, J.-H.1    Chung, T.D.Y.2    Oldenburg, K.R.3
  • 30
    • 84856292019 scopus 로고    scopus 로고
    • Catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate
    • Xue Y, Ha Y (2012) Catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate. J Biol Chem 287(5):3099-3107.
    • (2012) J Biol Chem , vol.287 , Issue.5 , pp. 3099-3107
    • Xue, Y.1    Ha, Y.2
  • 32
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Kolb HC, Finn MG, Sharpless KB (2001) Click chemistry: Diverse chemical function from a few good reactions. Angew Chem Int Ed Engl 40(11):2004-2021.
    • (2001) Angew Chem Int Ed Engl , vol.40 , Issue.11 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 33
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • DOI 10.1021/ja034490h
    • Speers AE, Adam GC, Cravatt BF (2003) Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. J Am Chem Soc 125(16):4686-4687. (Pubitemid 36505343)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.16 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 34
    • 0027934803 scopus 로고
    • Characterization of aarA, a pleiotrophic negative regulator of the 2'-N- Acetyltransferase in Providencia stuartii
    • Rather PN, Orosz E (1994) Characterization of aarA, a pleiotrophic negative regulator of the 2′-N-acetyltransferase in Providencia stuartii. J Bacteriol 176(16):5140-5144. (Pubitemid 24253759)
    • (1994) Journal of Bacteriology , vol.176 , Issue.16 , pp. 5140-5144
    • Rather, P.N.1    Orosz, E.2
  • 35
    • 71149098713 scopus 로고    scopus 로고
    • Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain
    • Sherratt AR, Braganza MV, Nguyen E, Ducat T, Goto NK (2009) Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain. Biochim Biophys Acta 1788(11):2444-2453.
    • (2009) Biochim Biophys Acta , vol.1788 , Issue.11 , pp. 2444-2453
    • Sherratt, A.R.1    Braganza, M.V.2    Nguyen, E.3    Ducat, T.4    Goto, N.K.5
  • 36
    • 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
    • Urban S, Freeman M (2003) Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain. Mol Cell 11(6):1425-1434. (Pubitemid 36776530)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 37
    • 72149124813 scopus 로고    scopus 로고
    • Sequence-specific intramembrane proteolysis: Identification of a recognition motif in rhomboid substrates
    • Strisovsky K, Sharpe HJ, Freeman M (2009) Sequence-specific intramembrane proteolysis: Identification of a recognition motif in rhomboid substrates. Mol Cell 36(6):1048-1059.
    • (2009) Mol Cell , vol.36 , Issue.6 , pp. 1048-1059
    • Strisovsky, K.1    Sharpe, H.J.2    Freeman, M.3
  • 38
    • 0012391933 scopus 로고
    • 3-Alkoxy-7-amino-4-chloroisocoumarins - A new class of suicide substrates for serine proteases
    • Harper JW, Powers JC (1984) 3-Alkoxy-7-amino-4-chloroisocoumarins - a new class of suicide substrates for serine proteases. J Am Chem Soc 106(24):7618-7619.
    • (1984) J Am Chem Soc , vol.106 , Issue.24 , pp. 7618-7619
    • Harper, J.W.1    Powers, J.C.2
  • 39
    • 0025265667 scopus 로고
    • Reaction of porcine pancreatic elastase with 7-substituted 3-alkoxy-4-chloroisocoumarins: Design of potent inhibitors using the crystal structure of the complex formed with 4-chloro-3-ethoxy-7-guanidinoisocoumarin
    • Powers JC, Oleksyszyn J, Narasimhan SL, Kam CM (1990) Reaction of porcine pancreatic elastase with 7-substituted 3-alkoxy-4-chloroisocoumarins: Design of potent inhibitors using the crystal structure of the complex formed with 4-chloro-3-ethoxy-7-guanidinoisocoumarin. Biochemistry 29(12):3108-3118. (Pubitemid 20119310)
    • (1990) Biochemistry , vol.29 , Issue.12 , pp. 3108-3118
    • Powers, J.C.1    Oleksyszyn, J.2    Narasimhan, S.L.3    Kam, C.-M.4    Radhakrishnan, R.5    Meyer Jr., E.F.6
  • 40
    • 0025980157 scopus 로고
    • Structural study of porcine pancreatic elastase complexed with 7-amino-3-(2-bromoethoxy)-4-chloroisocoumarin as a nonreactivatable doubly covalent enzyme-inhibitor complex
    • Vijayalakshmi J, Meyer EF, Jr., Kam CM, Powers JC (1991) Structural study of porcine pancreatic elastase complexed with 7-amino-3-(2-bromoethoxy)-4- chloroisocoumarin as a nonreactivatable doubly covalent enzyme-inhibitor complex. Biochemistry 30(8):2175-2183.
    • (1991) Biochemistry , vol.30 , Issue.8 , pp. 2175-2183
    • Vijayalakshmi, J.1    Meyer Jr., E.F.2    Kam, C.M.3    Powers, J.C.4
  • 41
    • 84855811087 scopus 로고    scopus 로고
    • Alkyne derivatives of isocoumarins as clickable activity-based probes for serine proteases
    • Haedke U, Götz M, Baer P, Verhelst SHL (2012) Alkyne derivatives of isocoumarins as clickable activity-based probes for serine proteases. Bioorg Med Chem 20(2):633-640.
    • (2012) Bioorg Med Chem , vol.20 , Issue.2 , pp. 633-640
    • Haedke, U.1    Götz, M.2    Baer, P.3    Verhelst, S.H.L.4
  • 42
    • 65549091985 scopus 로고    scopus 로고
    • Synthesis of beta-aminoethanesulfonyl fluorides or 2-substituted taurine sulfonyl fluorides as potential protease inhibitors
    • Brouwer AJ, Ceylan T, van der Linden T, Liskamp RMJ (2009) Synthesis of beta-aminoethanesulfonyl fluorides or 2-substituted taurine sulfonyl fluorides as potential protease inhibitors. Tetrahedron Lett 50(26):3391-3393.
    • (2009) Tetrahedron Lett , vol.50 , Issue.26 , pp. 3391-3393
    • Brouwer, A.J.1    Ceylan, T.2    Van Der Linden, T.3    Liskamp, R.M.J.4
  • 43
    • 79953221417 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of novel irreversible serine protease inhibitors using amino acid based sulfonyl fluorides as an electrophilic trap
    • Brouwer AJ, Ceylan T, Jonker AM, van der Linden T, Liskamp RMJ (2011) Synthesis and biological evaluation of novel irreversible serine protease inhibitors using amino acid based sulfonyl fluorides as an electrophilic trap. Bioorg Med Chem 19(7):2397-2406.
    • (2011) Bioorg Med Chem , vol.19 , Issue.7 , pp. 2397-2406
    • Brouwer, A.J.1    Ceylan, T.2    Jonker, A.M.3    Van Der Linden, T.4    Liskamp, R.M.J.5


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