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Volumn 523, Issue 7558, 2015, Pages 101-105

Cytosolic extensions directly regulate a rhomboid protease by modulating substrate gating

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM IONOPHORE; LIPOSOME; PROTEINASE; DROSOPHILA PROTEIN; MEMBRANE PROTEIN; PEPTIDE HYDROLASE;

EID: 84962422620     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14357     Document Type: Article
Times cited : (29)

References (32)
  • 1
    • 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).
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 2
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent c-secretase-like proteasemediates release of Notch intracellular domain
    • De Strooper, B. et al. A presenilin-1-dependent c-secretase-like proteasemediates release of Notch intracellular domain. Nature 398, 518-522 (1999).
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1
  • 3
    • 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
  • 4
    • 79955663580 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis-lessons from amyloid precursor protein processing
    • Lichtenthaler, S. F., Haass, C., Steiner, H. Regulated intramembrane proteolysis-lessons from amyloid precursor protein processing. J. Neurochem. 117, 779-796 (2011).
    • (2011) J. Neurochem , vol.117 , pp. 779-796
    • Lichtenthaler, S.F.1    Haass, C.2    Steiner, H.3
  • 5
    • 84861194622 scopus 로고    scopus 로고
    • The mechanism of c-secretase dysfunction in familial Alzheimer disease
    • Chavez-Gutierrez, L. et al. The mechanism of c-secretase dysfunction in familial Alzheimer disease. EMBO J. 31, 2261-2274 (2012).
    • (2012) EMBO J , vol.31 , pp. 2261-2274
    • Chavez-Gutierrez, L.1
  • 7
    • 67349117281 scopus 로고    scopus 로고
    • Making the cut: Central roles of intramembrane proteolysis in pathogenic microorganisms
    • Urban, S. Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms. Nature Rev. Microbiol. 7, 411-423 (2009).
    • (2009) Nature Rev. Microbiol , vol.7 , pp. 411-423
    • Urban, S.1
  • 8
    • 0037102238 scopus 로고    scopus 로고
    • A family of rhomboid intramembrane proteases activates all membrane-tether EGF ligands in Drosophila
    • Urban, S., Lee, J. R., Freeman, M. A family of rhomboid intramembrane proteases activates all membrane-tether EGF ligands in Drosophila. EMBO J. 21, 4277-4286 (2002).
    • (2002) EMBO J. , vol.21 , pp. 4277-4286
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 9
    • 33750465167 scopus 로고    scopus 로고
    • Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages ofmalaria
    • Baker, R. P., Wijetilaka, R., Urban, S. Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages ofmalaria. PLoS Pathog. 2, 922-932 (2006).
    • (2006) PLoS Pathog , vol.2 , pp. 922-932
    • Baker, R.P.1    Wijetilaka, R.2    Urban, S.3
  • 10
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin, S. M. et al. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 191, 933-942 (2010).
    • (2010) J. Cell Biol , vol.191 , pp. 933-942
    • Jin, S.M.1
  • 11
    • 84885187600 scopus 로고    scopus 로고
    • Protein trafficking and maturation regulate intramembrane proteolysis
    • Morohashi, Y., Tomita, T. Protein trafficking and maturation regulate intramembrane proteolysis. Biochim. Biophys. Acta 1828, 2855-2861 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2855-2861
    • Morohashi, Y.1    Tomita, T.2
  • 12
    • 84885161299 scopus 로고    scopus 로고
    • Untangling structure-function relationships in the rhomboid family of intramembrane proteases
    • Brooks, C. L., Lemieux, M. J. Untangling structure-function relationships in the rhomboid family of intramembrane proteases. Biochim. Biophys. Acta 1828, 2862-2872 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2862-2872
    • Brooks, C.L.1    Lemieux, M.J.2
  • 14
    • 84865328335 scopus 로고    scopus 로고
    • Architectural and thermodynamic principles underlying intramembrane protease function
    • Baker, R. P., Urban, S. Architectural and thermodynamic principles underlying intramembrane protease function. Nature Chem. Biol. 8, 759-768 (2012).
    • (2012) Nature Chem. Biol , vol.8 , pp. 759-768
    • Baker, R.P.1    Urban, S.2
  • 15
    • 84865389259 scopus 로고    scopus 로고
    • Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins
    • Fleig, L. et al. Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins. Mol. Cell 47, 558-569 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 558-569
    • Fleig, L.1
  • 16
    • 84890087383 scopus 로고    scopus 로고
    • Proteolysis inside the membrane is a rate-governed reaction not driven by substrate affinity
    • Dickey, S. W., Baker, R. P., Cho, S., Urban, S. Proteolysis inside the membrane is a rate-governed reaction not driven by substrate affinity. Cell 155, 1270-1281 (2013).
    • (2013) Cell , vol.155 , pp. 1270-1281
    • Dickey, S.W.1    Baker, R.P.2    Cho, S.3    Urban, S.4
  • 17
    • 84865574683 scopus 로고    scopus 로고
    • Oligomeric state study of prokaryotic rhomboid proteases
    • Sampathkumar, P. et al. Oligomeric state study of prokaryotic rhomboid proteases. Biochim. Biophys. Acta 1818, 3090-3097 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 3090-3097
    • Sampathkumar, P.1
  • 18
    • 0037040423 scopus 로고    scopus 로고
    • A Ca21 switch aligns the active site of calpain
    • Moldoveanu, T. et al. A Ca21 switch aligns the active site of calpain. Cell 108, 649-660 (2002).
    • (2002) Cell , vol.108 , pp. 649-660
    • Moldoveanu, T.1
  • 19
    • 84878843045 scopus 로고    scopus 로고
    • Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics
    • Moin, S. M., Urban, S. Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics. eLife 1, e00173 (2012).
    • (2012) ELife , vol.1 , pp. e00173
    • Moin, S.M.1    Urban, S.2
  • 20
    • 50849109498 scopus 로고    scopus 로고
    • Vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells
    • Urban, S., Baker, R. P. In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells. Biol. Chem. 389, 1107-1115 (2008).
    • (2008) Biol. Chem , vol.389 , pp. 1107-1115
    • Urban, S.1    Baker, R.P.2
  • 21
    • 84878409837 scopus 로고    scopus 로고
    • Large lateral movement of transmembrane helix S5 is not required for substrate access to the active site of rhomboid intramembrane protease
    • Xue, Y., Ha, Y. Large lateral movement of transmembrane helix S5 is not required for substrate access to the active site of rhomboid intramembrane protease. J. Biol. Chem. 288, 16645-16654 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 16645-16654
    • Xue, Y.1    Ha, Y.2
  • 22
    • 72149124813 scopus 로고    scopus 로고
    • Sequence-specific intramembrane proteolysis: Identification of a recognition motif in rhomboid substrates
    • Strisovsky, K., Sharpe, H. J., Freeman, M. Sequence-specific intramembrane proteolysis: identification of a recognition motif in rhomboid substrates. Mol. Cell 36, 1048-1059 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 1048-1059
    • Strisovsky, K.1    Sharpe, H.J.2    Freeman, M.3
  • 23
    • 61549125968 scopus 로고    scopus 로고
    • Rhomboid protease dynamics and lipid interactions
    • Bondar, A. N., del Val, C., White, S. H. Rhomboid protease dynamics and lipid interactions. Structure 17, 395-405 (2009).
    • (2009) Structure , vol.17 , pp. 395-405
    • Bondar, A.N.1    Del Val, C.2    White, S.H.3
  • 24
    • 0035282457 scopus 로고    scopus 로고
    • Synaptotagmin i functions as a calcium regulator of release probability
    • Fernandez-Chacon, R. et al. Synaptotagmin I functions as a calcium regulator of release probability. Nature 410, 41-49 (2001).
    • (2001) Nature , vol.410 , pp. 41-49
    • Fernandez-Chacon, R.1
  • 25
    • 0036127811 scopus 로고    scopus 로고
    • Cloning and expression of Ventrhoid, a novel vertebrate homologue of the Drosophila EGFpathway gene rhomboid
    • Jaszai, J., Brand, M. Cloning and expression of Ventrhoid, a novel vertebrate homologue of the Drosophila EGFpathway gene rhomboid. Mech. Dev. 113, 73-77 (2002).
    • (2002) Mech. Dev , vol.113 , pp. 73-77
    • Jaszai, J.1    Brand, M.2
  • 26
    • 9144227397 scopus 로고    scopus 로고
    • Mental retardation and cardiovascular malformations in NF1 microdeleted patients point to candidate genes in 17q11 2
    • Venturin, M. et al. Mental retardation and cardiovascular malformations in NF1 microdeleted patients point to candidate genes in 17q11.2. J. Med. Genet. 41, 35-41 (2004).
    • (2004) J. Med. Genet , vol.41 , pp. 35-41
    • Venturin, M.1
  • 27
    • 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).
    • (2003) Genome Biol , vol.4 , pp. R19
    • Koonin, E.V.1
  • 28
    • 41849117736 scopus 로고    scopus 로고
    • Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii
    • Sheiner, L., Dowse, T. J., Soldati-Favre, D. Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii. Traffic 9, 665-677 (2008).
    • (2008) Traffic , vol.9 , pp. 665-677
    • Sheiner, L.1    Dowse, T.J.2    Soldati-Favre, D.3
  • 29
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • Feng, L. et al. Structure of a site-2 protease family intramembrane metalloprotease. Science 318, 1608-1612 (2007).
    • (2007) Science , vol.318 , pp. 1608-1612
    • Feng, L.1
  • 30
    • 84871725890 scopus 로고    scopus 로고
    • Structure of a presenilin family intramembrane aspartate protease
    • Li, X. et al. Structure of a presenilin family intramembrane aspartate protease. Nature 493, 56-61 (2013).
    • (2013) Nature , vol.493 , pp. 56-61
    • Li, X.1
  • 31
    • 13844306483 scopus 로고    scopus 로고
    • Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity
    • Urban, S., Wolfe, M. S. Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity. Proc. Natl Acad. Sci. USA 102, 1883-1888 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1883-1888
    • Urban, S.1    Wolfe, M.S.2
  • 32
    • 34347250499 scopus 로고    scopus 로고
    • Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate
    • Baker, R. P., Young, K., Feng, L., Shi, Y., Urban, S. Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate. Proc. Natl Acad. Sci. USA 104, 8257-8262 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 8257-8262
    • Baker, R.P.1    Young, K.2    Feng, L.3    Shi, Y.4    Urban, S.5


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