메뉴 건너뛰기




Volumn 277, Issue 15, 2010, Pages 3158-3175

Golgi reassembly stacking protein 55 interacts with membrane-type (MT) 1-matrix metalloprotease (MMP) and furin and plays a role in the activation of the MT1-MMP zymogen

Author keywords

furin; GRASP55; intracellular traffic; MT1 MMP; protease

Indexed keywords

ENZYME PRECURSOR; FURIN; GOLGI REASSEMBLY STACKING PROTEIN 55; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE 15; MATRIX METALLOPROTEINASE 16; MATRIX PROTEIN; METALLOPROTEINASE; MT5 MMP; PROTEINASE; UNCLASSIFIED DRUG;

EID: 77954717764     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07723.x     Document Type: Article
Times cited : (30)

References (73)
  • 3
    • 0033230113 scopus 로고    scopus 로고
    • Membrane associated matrix metalloproteinases in metastasis
    • Ellerbroek SM Stack MS (1999) Membrane associated matrix metalloproteinases in metastasis. Bioessays 21, 940 949.
    • (1999) Bioessays , vol.21 , pp. 940-949
    • Ellerbroek, S.M.1    Stack, M.S.2
  • 4
    • 20044387216 scopus 로고    scopus 로고
    • Roles of membrane-type matrix metalloproteinase-1 in tumor invasion and metastasis
    • Sato H, Takino T Miyamori H (2005) Roles of membrane-type matrix metalloproteinase-1 in tumor invasion and metastasis. Cancer Sci 96, 212 217.
    • (2005) Cancer Sci , vol.96 , pp. 212-217
    • Sato, H.1    Takino, T.2    Miyamori, H.3
  • 5
    • 28444454893 scopus 로고    scopus 로고
    • MT1-MMP: A potent modifier of pericellular microenvironment
    • Itoh Y Seiki M (2006) MT1-MMP: a potent modifier of pericellular microenvironment. J Cell Physiol 206, 1 8.
    • (2006) J Cell Physiol , vol.206 , pp. 1-8
    • Itoh, Y.1    Seiki, M.2
  • 6
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3
    • Will H, Atkinson SJ, Butler GS, Smith B Murphy G (1996) The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. J Biol Chem 271, 17119 17123.
    • (1996) J Biol Chem , vol.271 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 7
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme
    • Knauper V, Will H, Lopez-Otin C, Smith B, Atkinson SJ, Stanton H, Hembry RM Murphy G (1996) Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme. J Biol Chem 271, 17124 17131.
    • (1996) J Biol Chem , vol.271 , pp. 17124-17131
    • Knauper, V.1    Will, H.2    Lopez-Otin, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 9
    • 0037426578 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion
    • Seiki M (2003) Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion. Cancer Lett 194, 1 11.
    • (2003) Cancer Lett , vol.194 , pp. 1-11
    • Seiki, M.1
  • 10
    • 0037052641 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer: Prognostic markers and therapeutic targets
    • Vihinen P Kahari VM (2002) Matrix metalloproteinases in cancer: prognostic markers and therapeutic targets. Int J Cancer 99, 157 166.
    • (2002) Int J Cancer , vol.99 , pp. 157-166
    • Vihinen, P.1    Kahari, V.M.2
  • 13
    • 0038784546 scopus 로고    scopus 로고
    • Membrane type i matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix
    • Hotary KB, Allen ED, Brooks PC, Datta NS, Long MW Weiss SJ (2003) Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix. Cell 114, 33 45.
    • (2003) Cell , vol.114 , pp. 33-45
    • Hotary, K.B.1    Allen, E.D.2    Brooks, P.C.3    Datta, N.S.4    Long, M.W.5    Weiss, S.J.6
  • 14
    • 0346363608 scopus 로고    scopus 로고
    • Sequence-specific silencing of MT1-MMP expression suppresses tumor cell migration and invasion: Importance of MT1-MMP as a therapeutic target for invasive tumors
    • Ueda J, Kajita M, Suenaga N, Fujii K Seiki M (2003) Sequence-specific silencing of MT1-MMP expression suppresses tumor cell migration and invasion: importance of MT1-MMP as a therapeutic target for invasive tumors. Oncogene 22, 8716 8722.
    • (2003) Oncogene , vol.22 , pp. 8716-8722
    • Ueda, J.1    Kajita, M.2    Suenaga, N.3    Fujii, K.4    Seiki, M.5
  • 15
    • 77049111600 scopus 로고    scopus 로고
    • Emerging concepts in the regulation of membrane-type 1 matrix metalloproteinase activity
    • Gingras D Beliveau R (2009) Emerging concepts in the regulation of membrane-type 1 matrix metalloproteinase activity. Biochim Biophys Acta 1803, 142 150.
    • (2009) Biochim Biophys Acta , vol.1803 , pp. 142-150
    • Gingras, D.1    Beliveau, R.2
  • 16
    • 0035955469 scopus 로고    scopus 로고
    • Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1 matrix metalloproteinase (MT1-MMP)
    • Gingras D, Bousquet-Gagnon N, Langlois S, Lachambre MP, Annabi B Beliveau R (2001) Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1 matrix metalloproteinase (MT1-MMP). FEBS Lett 507, 231 236.
    • (2001) FEBS Lett , vol.507 , pp. 231-236
    • Gingras, D.1    Bousquet-Gagnon, N.2    Langlois, S.3    Lachambre, M.P.4    Annabi, B.5    Beliveau, R.6
  • 17
    • 0034685778 scopus 로고    scopus 로고
    • Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain
    • Lehti K, Valtanen H, Wickstrom SA, Lohi J Keski-Oja J (2000) Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain. J Biol Chem 275, 15006 15013.
    • (2000) J Biol Chem , vol.275 , pp. 15006-15013
    • Lehti, K.1    Valtanen, H.2    Wickstrom, S.A.3    Lohi, J.4    Keski-Oja, J.5
  • 18
    • 0035945354 scopus 로고    scopus 로고
    • Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity
    • Uekita T, Itoh Y, Yana I, Ohno H Seiki M (2001) Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity. J Cell Biol 155, 1345 1356.
    • (2001) J Cell Biol , vol.155 , pp. 1345-1356
    • Uekita, T.1    Itoh, Y.2    Yana, I.3    Ohno, H.4    Seiki, M.5
  • 19
    • 0032921863 scopus 로고    scopus 로고
    • The cytoplasmic carboxy-terminal amino acid determines the subcellular localization of proTGF-(alpha) and membrane type matrix metalloprotease (MT1-MMP)
    • Urena JM, Merlos-Suarez A, Baselga J Arribas J (1999) The cytoplasmic carboxy-terminal amino acid determines the subcellular localization of proTGF-(alpha) and membrane type matrix metalloprotease (MT1-MMP). J Cell Sci 112, 773 784.
    • (1999) J Cell Sci , vol.112 , pp. 773-784
    • Urena, J.M.1    Merlos-Suarez, A.2    Baselga, J.3    Arribas, J.4
  • 20
    • 0035923669 scopus 로고    scopus 로고
    • Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis
    • Jiang A, Lehti K, Wang X, Weiss SJ, Keski-Oja J Pei D (2001) Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis. Proc Natl Acad Sci USA 98, 13693 13698.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13693-13698
    • Jiang, A.1    Lehti, K.2    Wang, X.3    Weiss, S.J.4    Keski-Oja, J.5    Pei, D.6
  • 21
    • 0037063349 scopus 로고    scopus 로고
    • The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein
    • Rozanov DV, Ghebrehiwet B, Ratnikov B, Monosov EZ, Deryugina EI Strongin AY (2002) The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein. FEBS Lett 527, 51 57.
    • (2002) FEBS Lett , vol.527 , pp. 51-57
    • Rozanov, D.V.1    Ghebrehiwet, B.2    Ratnikov, B.3    Monosov, E.Z.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 22
    • 0142011033 scopus 로고    scopus 로고
    • Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface
    • Remacle A, Murphy G Roghi C (2003) Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface. J Cell Sci 116, 3905 3916.
    • (2003) J Cell Sci , vol.116 , pp. 3905-3916
    • Remacle, A.1    Murphy, G.2    Roghi, C.3
  • 23
    • 1542304781 scopus 로고    scopus 로고
    • Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal
    • Wang X, Ma D, Keski-Oja J Pei D (2004) Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal. J Biol Chem 279, 9331 9336.
    • (2004) J Biol Chem , vol.279 , pp. 9331-9336
    • Wang, X.1    Ma, D.2    Keski-Oja, J.3    Pei, D.4
  • 24
    • 0030791315 scopus 로고    scopus 로고
    • Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion
    • Nakahara H, Howard L, Thompson EW, Sato H, Seiki M, Yeh Y Chen WT (1997) Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion. Proc Natl Acad Sci USA 94, 7959 7964.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7959-7964
    • Nakahara, H.1    Howard, L.2    Thompson, E.W.3    Sato, H.4    Seiki, M.5    Yeh, Y.6    Chen, W.T.7
  • 26
    • 38049174649 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-2 binding to membrane-type 1 matrix metalloproteinase induces MAPK activation and cell growth by a non-proteolytic mechanism
    • D'Alessio S, Ferrari G, Cinnante K, Scheerer W, Galloway AC, Roses DF, Rozanov DV, Remacle AG, Oh ES, Shiryaev SA et al. (2008) Tissue inhibitor of metalloproteinases-2 binding to membrane-type 1 matrix metalloproteinase induces MAPK activation and cell growth by a non-proteolytic mechanism. J Biol Chem 283, 87 99.
    • (2008) J Biol Chem , vol.283 , pp. 87-99
    • D'Alessio, S.1    Ferrari, G.2    Cinnante, K.3    Scheerer, W.4    Galloway, A.C.5    Roses, D.F.6    Rozanov, D.V.7    Remacle, A.G.8    Oh, E.S.9    Shiryaev, S.A.10
  • 28
    • 0037040914 scopus 로고    scopus 로고
    • Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase
    • Lehti K, Lohi J, Juntunen MM, Pei D Keski-Oja J (2002) Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase. J Biol Chem 277, 8440 8448.
    • (2002) J Biol Chem , vol.277 , pp. 8440-8448
    • Lehti, K.1    Lohi, J.2    Juntunen, M.M.3    Pei, D.4    Keski-Oja, J.5
  • 29
    • 58149093961 scopus 로고    scopus 로고
    • The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase
    • Ludwig T, Theissen SM, Morton MJ Caplan MJ (2008) The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase. J Biol Chem 283, 35410 35418.
    • (2008) J Biol Chem , vol.283 , pp. 35410-35418
    • Ludwig, T.1    Theissen, S.M.2    Morton, M.J.3    Caplan, M.J.4
  • 30
    • 23444460823 scopus 로고    scopus 로고
    • Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration
    • Anilkumar N, Uekita T, Couchman JR, Nagase H, Seiki M Itoh Y (2005) Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. FASEB J 19, 1326 1328.
    • (2005) FASEB J , vol.19 , pp. 1326-1328
    • Anilkumar, N.1    Uekita, T.2    Couchman, J.R.3    Nagase, H.4    Seiki, M.5    Itoh, Y.6
  • 31
    • 34447522132 scopus 로고    scopus 로고
    • Src-dependent phosphorylation of membrane type i matrix metalloproteinase on cytoplasmic tyrosine 573: Role in endothelial and tumour cell migration
    • Nyalendo C, Michaud M, Beaulieu E, Roghi C, Murphy G, Gingras D Beliveau R (2007) Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumour cell migration. J Biol Chem 282, 15690 15699.
    • (2007) J Biol Chem , vol.282 , pp. 15690-15699
    • Nyalendo, C.1    Michaud, M.2    Beaulieu, E.3    Roghi, C.4    Murphy, G.5    Gingras, D.6    Beliveau, R.7
  • 32
    • 67749137602 scopus 로고    scopus 로고
    • Modulation of the membrane type 1 matrix metalloproteinase cytoplasmic tail enhances tumor cell invasion and proliferation in three-dimensional collagen matrices
    • Moss NMP, Wu YIP, Liu YM, Munshi HGM Stack MSP (2009) Modulation of the membrane type 1 matrix metalloproteinase cytoplasmic tail enhances tumor cell invasion and proliferation in three-dimensional collagen matrices. J Biol Chem 284, 19791 19799.
    • (2009) J Biol Chem , vol.284 , pp. 19791-19799
    • Moss, N.M.P.1    Wu, Y.I.P.2    Liu, Y.M.3    Munshi, H.G.M.4    Stack, M.S.P.5
  • 33
    • 1842581954 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the Cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumors
    • Uekita T, Gotoh I, Kinoshita T, Itoh Y, Sato H, Shiomi T, Okada Y Seiki M (2004) Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the Cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumors. J Biol Chem 279, 12734 12743.
    • (2004) J Biol Chem , vol.279 , pp. 12734-12743
    • Uekita, T.1    Gotoh, I.2    Kinoshita, T.3    Itoh, Y.4    Sato, H.5    Shiomi, T.6    Okada, Y.7    Seiki, M.8
  • 34
    • 10644229956 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase
    • Labrecque L, Nyalendo C, Langlois S, Durocher Y, Roghi C, Murphy G, Gingras D Beliveau R (2004) Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase. J Biol Chem 279, 52132 52140.
    • (2004) J Biol Chem , vol.279 , pp. 52132-52140
    • Labrecque, L.1    Nyalendo, C.2    Langlois, S.3    Durocher, Y.4    Roghi, C.5    Murphy, G.6    Gingras, D.7    Beliveau, R.8
  • 35
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • Shorter J, Watson R, Giannakou ME, Clarke M, Warren G Barr FA (1999) GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J 18, 4949 4960.
    • (1999) EMBO J , vol.18 , pp. 4949-4960
    • Shorter, J.1    Watson, R.2    Giannakou, M.E.3    Clarke, M.4    Warren, G.5    Barr, F.A.6
  • 37
    • 0034423410 scopus 로고    scopus 로고
    • Transmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55
    • Kuo A, Zhong C, Lane WS Derynck R (2000) Transmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55. EMBO J 19, 6427 6439.
    • (2000) EMBO J , vol.19 , pp. 6427-6439
    • Kuo, A.1    Zhong, C.2    Lane, W.S.3    Derynck, R.4
  • 39
    • 0035842897 scopus 로고    scopus 로고
    • Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus
    • Barr FA, Preisinger C, Kopajtich R Korner R (2001) Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus. J Cell Biol 155, 885 891.
    • (2001) J Cell Biol , vol.155 , pp. 885-891
    • Barr, F.A.1    Preisinger, C.2    Kopajtich, R.3    Korner, R.4
  • 40
    • 0035167603 scopus 로고    scopus 로고
    • Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2
    • Jesch SA, Lewis TS, Ahn NG Linstedt AD (2001) Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2. Mol Biol Cell 12, 1811 1817.
    • (2001) Mol Biol Cell , vol.12 , pp. 1811-1817
    • Jesch, S.A.1    Lewis, T.S.2    Ahn, N.G.3    Linstedt, A.D.4
  • 41
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • Barr FA, Puype M, Vandekerckhove J Warren G (1997) GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91, 253 262.
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 42
    • 0033944447 scopus 로고    scopus 로고
    • Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases
    • Yana I Weiss SJ (2000) Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases. Mol Biol Cell 11, 2387 2401.
    • (2000) Mol Biol Cell , vol.11 , pp. 2387-2401
    • Yana, I.1    Weiss, S.J.2
  • 43
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • Nakayama K (1997) Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem J 327, 625 635.
    • (1997) Biochem J , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 44
    • 33748644942 scopus 로고    scopus 로고
    • Furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP
    • Remacle AG, Rozanov DV, Fugere M, Day R Strongin AY (2006) Furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP. Oncogene 25, 5648 5655.
    • (2006) Oncogene , vol.25 , pp. 5648-5655
    • Remacle, A.G.1    Rozanov, D.V.2    Fugere, M.3    Day, R.4    Strongin, A.Y.5
  • 45
  • 47
    • 0030273552 scopus 로고    scopus 로고
    • + channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation
    • + channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation. Neuron 17, 759 767.
    • (1996) Neuron , vol.17 , pp. 759-767
    • Cohen, N.A.1    Brenman, J.E.2    Snyder, S.H.3    Bredt, D.S.4
  • 48
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor
    • Cao TT, Deacon HW, Reczek D, Bretscher A von Zastrow M (1999) A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor. Nature 401, 286 290.
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3    Bretscher, A.4    Von Zastrow, M.5
  • 50
    • 0037449799 scopus 로고    scopus 로고
    • Novel mode of ligand recognition by the Erbin PDZ domain
    • Birrane G, Chung J Ladias JA (2003) Novel mode of ligand recognition by the Erbin PDZ domain. J Biol Chem 278, 1399 1402.
    • (2003) J Biol Chem , vol.278 , pp. 1399-1402
    • Birrane, G.1    Chung, J.2    Ladias, J.A.3
  • 54
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • Itoh Y, Takamura A, Ito N, Maru Y, Sato H, Suenaga N, Aoki T Seiki M (2001) Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J 20, 4782 4793.
    • (2001) EMBO J , vol.20 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6    Aoki, T.7    Seiki, M.8
  • 56
    • 0032572532 scopus 로고    scopus 로고
    • Coordination of an array of signaling proteins through homo- and heteromeric interactions between PDZ domains and target proteins
    • Xu XZ, Choudhury A, Li X Montell C (1998) Coordination of an array of signaling proteins through homo- and heteromeric interactions between PDZ domains and target proteins. J Cell Biol 142, 545 555.
    • (1998) J Cell Biol , vol.142 , pp. 545-555
    • Xu, X.Z.1    Choudhury, A.2    Li, X.3    Montell, C.4
  • 57
    • 0030921919 scopus 로고    scopus 로고
    • Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95
    • Hsueh YP, Kim E Sheng M (1997) Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95. Neuron 18, 803 814.
    • (1997) Neuron , vol.18 , pp. 803-814
    • Hsueh, Y.P.1    Kim, E.2    Sheng, M.3
  • 58
    • 0037926394 scopus 로고    scopus 로고
    • A direct role for GRASP65 as a mitotically regulated Golgi stacking factor
    • Wang Y, Seemann J, Pypaert M, Shorter J Warren G (2003) A direct role for GRASP65 as a mitotically regulated Golgi stacking factor. EMBO J 22, 3279 3290.
    • (2003) EMBO J , vol.22 , pp. 3279-3290
    • Wang, Y.1    Seemann, J.2    Pypaert, M.3    Shorter, J.4    Warren, G.5
  • 60
    • 4344672352 scopus 로고    scopus 로고
    • Prointegrin maturation follows rapid trafficking and processing of MT1-MMP in furin-negative colon carcinoma LoVo cells
    • Deryugina EI, Ratnikov BI, Yu Q, Baciu PC, Rozanov DV Strongin AY (2004) Prointegrin maturation follows rapid trafficking and processing of MT1-MMP in furin-negative colon carcinoma LoVo cells. Traffic 5, 627 641.
    • (2004) Traffic , vol.5 , pp. 627-641
    • Deryugina, E.I.1    Ratnikov, B.I.2    Yu, Q.3    Baciu, P.C.4    Rozanov, D.V.5    Strongin, A.Y.6
  • 61
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity
    • Pei D Weiss SJ (1996) Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J Biol Chem 271, 9135 9140.
    • (1996) J Biol Chem , vol.271 , pp. 9135-9140
    • Pei, D.1    Weiss, S.J.2
  • 62
    • 20344368596 scopus 로고    scopus 로고
    • Furin-like proprotein convertases are central regulators of the membrane type matrix metalloproteinase-pro-matrix metalloproteinase-2 proteolytic cascade in atherosclerosis
    • Stawowy P, Meyborg H, Stibenz D, Borges Pereira Stawowy N, Roser M, Thanabalasingam U, Veinot JP, Chretien M, Seidah NG, Fleck E et al. (2005) Furin-like proprotein convertases are central regulators of the membrane type matrix metalloproteinase-pro-matrix metalloproteinase-2 proteolytic cascade in atherosclerosis. Circulation 111, 2820 2827.
    • (2005) Circulation , vol.111 , pp. 2820-2827
    • Stawowy, P.1    Meyborg, H.2    Stibenz, D.3    Borges Pereira Stawowy, N.4    Roser, M.5    Thanabalasingam, U.6    Veinot, J.P.7    Chretien, M.8    Seidah, N.G.9    Fleck, E.10
  • 63
    • 0036468911 scopus 로고    scopus 로고
    • Activation of membrane-type matrix metalloproteinase 3 zymogen by the proprotein convertase furin in the trans-Golgi network
    • Kang T, Nagase H Pei D (2002) Activation of membrane-type matrix metalloproteinase 3 zymogen by the proprotein convertase furin in the trans-Golgi network. Cancer Res 62, 675 681.
    • (2002) Cancer Res , vol.62 , pp. 675-681
    • Kang, T.1    Nagase, H.2    Pei, D.3
  • 64
    • 0035929618 scopus 로고    scopus 로고
    • Shedding of membrane type matrix metalloproteinase 5 by a furin-type convertase: A potential mechanism for down-regulation
    • Wang X Pei D (2001) Shedding of membrane type matrix metalloproteinase 5 by a furin-type convertase: a potential mechanism for down-regulation. J Biol Chem 276, 35953 35960.
    • (2001) J Biol Chem , vol.276 , pp. 35953-35960
    • Wang, X.1    Pei, D.2
  • 65
    • 0029133344 scopus 로고
    • CDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment
    • Will H Hinzmann B (1995) cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur J Biochem 231, 602 608.
    • (1995) Eur J Biochem , vol.231 , pp. 602-608
    • Will, H.1    Hinzmann, B.2
  • 66
    • 2442561408 scopus 로고    scopus 로고
    • Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV
    • Wang P, Wang X Pei D (2004) Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV. J Biol Chem 279, 20461 20470.
    • (2004) J Biol Chem , vol.279 , pp. 20461-20470
    • Wang, P.1    Wang, X.2    Pei, D.3
  • 67
    • 33645644482 scopus 로고    scopus 로고
    • Membrane localization of membrane type 5 matrix metalloproteinase by AMPA receptor binding protein and cleavage of cadherins
    • Monea S, Jordan BA, Srivastava S, DeSouza S Ziff EB (2006) Membrane localization of membrane type 5 matrix metalloproteinase by AMPA receptor binding protein and cleavage of cadherins. J Neurosci 26, 2300 2312.
    • (2006) J Neurosci , vol.26 , pp. 2300-2312
    • Monea, S.1    Jordan, B.A.2    Srivastava, S.3    Desouza, S.4    Ziff, E.B.5
  • 68
    • 0242710747 scopus 로고    scopus 로고
    • TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity
    • Srour N, Lebel A, McMahon S, Fournier I, Fugere M, Day R Dubois CM (2003) TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity. FEBS Lett 554, 275 283.
    • (2003) FEBS Lett , vol.554 , pp. 275-283
    • Srour, N.1    Lebel, A.2    McMahon, S.3    Fournier, I.4    Fugere, M.5    Day, R.6    Dubois, C.M.7
  • 69
    • 33747176841 scopus 로고    scopus 로고
    • MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells
    • Atkinson SJ, Roghi C Murphy G (2006) MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells. Biochem J 398, 15 22.
    • (2006) Biochem J , vol.398 , pp. 15-22
    • Atkinson, S.J.1    Roghi, C.2    Murphy, G.3
  • 70
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer A, Fransen JA, Bachi T, Ginsel L Hauri HP (1988) Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J Cell Biol 107, 1643 1653.
    • (1988) J Cell Biol , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.2    Bachi, T.3    Ginsel, L.4    Hauri, H.P.5
  • 72
    • 0035868365 scopus 로고    scopus 로고
    • 'Shed' furin: Mapping of the cleavage determinants and identification of its C-terminus
    • Plaimauer B, Mohr G, Wernhart W, Himmelspach M, Dorner F Schlokat U (2001) 'Shed' furin: mapping of the cleavage determinants and identification of its C-terminus. Biochem J 354, 689 695.
    • (2001) Biochem J , vol.354 , pp. 689-695
    • Plaimauer, B.1    Mohr, G.2    Wernhart, W.3    Himmelspach, M.4    Dorner, F.5    Schlokat, U.6
  • 73
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen C Dowdle EB (1980) Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal Biochem 102, 196 202.
    • (1980) Anal Biochem , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.