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Volumn 69, Issue 13, 2012, Pages 2233-2244

Palmitoylation by DHHC3 is critical for the function, expression, and stability of integrin α6β4

Author keywords

6 4; DHHC3; Integrin; Palmitoylation

Indexed keywords

ACYLTRANSFERASE; ALPHA6 INTEGRIN; ALPHA6BETA4 INTEGRIN; BETA4 INTEGRIN; CATHEPSIN D; MEMBRANE ENZYME; PEPSTATIN; PROTEIN DHHC3; UNCLASSIFIED DRUG;

EID: 84862897870     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-0924-6     Document Type: Article
Times cited : (48)

References (55)
  • 1
    • 0035658282 scopus 로고    scopus 로고
    • Traction forces mediated by α6β4 integrin: Implications for basement membrane organization and tumor invasion
    • I Rabinovitz IK Gipson AM Mercurio 2001 Traction forces mediated by alpha6beta4 integrin: implications for basement membrane organization and tumor invasion Mol Biol Cell 12 4030 4043 1:CAS:528:DC%2BD3MXpt1Giu7o%3D 11739798 (Pubitemid 34001090)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.12 , pp. 4030-4043
    • Rabinovitz, I.1    Gipson, I.K.2    Mercurio, A.M.3
  • 2
    • 85046914504 scopus 로고    scopus 로고
    • Advances and perspectives of the architecture of hemidesmosomes: Lessons from structural biology
    • 10.4161/cam.3.4.9525 19736524
    • JM de Pereda E Ortega N Alonso-Garcia M Gomez-Hernandez A Sonnenberg 2009 Advances and perspectives of the architecture of hemidesmosomes: lessons from structural biology Cell Adh Migr 3 361 364 10.4161/cam.3.4.9525 19736524
    • (2009) Cell Adh Migr , vol.3 , pp. 361-364
    • De Pereda, J.M.1    Ortega, E.2    Alonso-Garcia, N.3    Gomez-Hernandez, M.4    Sonnenberg, A.5
  • 3
    • 0029908558 scopus 로고    scopus 로고
    • Absence of integrin α6 leads to epidermolysis bullosa and neonatal death in mice
    • DOI 10.1038/ng0796-370
    • EN Georges-Labouesse N Messaddeq G Yehia L Cadalbert A Dierich M Le Meur 1996 Absence of the alpha-6 integrin leads to epidermolysis bullosa and neonatal death in mice Nat Genet 13 370 373 10.1038/ng0796-370 1:STN:280: DyaK283lvFGksg%3D%3D 8673141 (Pubitemid 26230508)
    • (1996) Nature Genetics , vol.13 , Issue.3 , pp. 370-373
    • Georges-Labouesse, E.1    Messaddeq, N.2    Yehia, G.3    Cadalbert, L.4    Dierich, A.5    Le Meur, M.6
  • 4
    • 0032962217 scopus 로고    scopus 로고
    • Mutation analysis and molecular genetics of epidermolysis bullosa
    • DOI 10.1016/S0945-053X(98)00005-5, PII S0945053X98000055
    • L Pulkkinen J Uitto 1999 Mutation analysis and molecular genetics of epidermolysis bullosa Matrix Biol 18 29 42 10.1016/S0945-053X(98)00005-5 1:CAS:528:DyaK1MXjsV2it7s%3D 10367729 (Pubitemid 29213825)
    • (1999) Matrix Biology , vol.18 , Issue.1 , pp. 29-42
    • Pulkkinen, L.1    Uitto, J.2
  • 5
    • 34447324354 scopus 로고    scopus 로고
    • Platelet integrins and immunoreceptors
    • DOI 10.1111/j.1600-065X.2007.00532.x
    • A Kasirer-Friede ML Kahn SJ Shattil 2007 Platelet integrins and immunoreceptors Immunol Rev 218 247 264 10.1111/j.1600-065X.2007.00532.x 1:CAS:528:DC%2BD2sXhtVSiu7zF 17624957 (Pubitemid 47052302)
    • (2007) Immunological Reviews , vol.218 , Issue.1 , pp. 247-264
    • Kasirer-Friede, A.1    Kahn, M.L.2    Shattil, S.J.3
  • 6
    • 1842734428 scopus 로고    scopus 로고
    • Positioning the immune system: Unexpected roles for α6-integrins
    • DOI 10.1111/j.0019-2805.2004.01838.x
    • G Borland W Cushley 2004 Positioning the immune system: unexpected roles for alpha6-integrins Immunology 111 381 383 10.1111/j.0019-2805.2004.01838.x 1:CAS:528:DC%2BD2cXjtlOjsbs%3D 15056373 (Pubitemid 38482488)
    • (2004) Immunology , vol.111 , Issue.4 , pp. 381-383
    • Borland, G.1    Cushley, W.2
  • 7
    • 50849132912 scopus 로고    scopus 로고
    • A role for the integrin alpha6beta1 in the differential distribution of CD4 and CD8 T-cell subsets within the rheumatoid synovium
    • 10.1093/rheumatology/ken263 1:CAS:528:DC%2BD1cXhtV2isbvF
    • O Haworth DL Hardie A Burman GE Rainger B Eksteen DH Adams M Salmon GB Nash CD Buckley 2008 A role for the integrin alpha6beta1 in the differential distribution of CD4 and CD8 T-cell subsets within the rheumatoid synovium Rheumatology (Oxford) 47 1329 1334 10.1093/rheumatology/ken263 1:CAS:528:DC%2BD1cXhtV2isbvF
    • (2008) Rheumatology (Oxford) , vol.47 , pp. 1329-1334
    • Haworth, O.1    Hardie, D.L.2    Burman, A.3    Rainger, G.E.4    Eksteen, B.5    Adams, D.H.6    Salmon, M.7    Nash, G.B.8    Buckley, C.D.9
  • 8
    • 0033181341 scopus 로고    scopus 로고
    • Expression of the α6 integrin confers papillomavirus binding upon receptor-negative B-cells
    • DOI 10.1006/viro.1999.9825
    • NA McMillan E Payne IH Frazer M Evander 1999 Expression of the alpha6 integrin confers papillomavirus binding upon receptor-negative B-cells Virology 261 271 279 10.1006/viro.1999.9825 1:CAS:528:DyaK1MXmtVygsbg%3D 10497112 (Pubitemid 29431779)
    • (1999) Virology , vol.261 , Issue.2 , pp. 271-279
    • McMillan, N.A.J.1    Payne, E.2    Frazer, I.H.3    Evander, M.4
  • 9
    • 27644496163 scopus 로고    scopus 로고
    • Mobilization and activation of a signaling competent α6β4 integrin underlies its contribution to carcinoma progression
    • DOI 10.1007/s10555-005-5133-4
    • EA Lipscomb AM Mercurio 2005 Mobilization and activation of a signaling competent alpha6beta4integrin underlies its contribution to carcinoma progression Cancer Metastasis Rev 24 413 423 10.1007/s10555-005-5133-4 1:CAS:528:DC%2BD2MXhtFKht73P 16258729 (Pubitemid 41569981)
    • (2005) Cancer and Metastasis Reviews , vol.24 , Issue.3 , pp. 413-423
    • Lipscomb, E.A.1    Mercurio, A.M.2
  • 10
    • 77953064012 scopus 로고    scopus 로고
    • Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets
    • 10.1017/S1462399409001355 20078909
    • CS Stipp 2010 Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets Expert Rev Mol Med 12 e3 10.1017/ S1462399409001355 20078909
    • (2010) Expert Rev Mol Med , vol.12 , pp. 3
    • Stipp, C.S.1
  • 11
    • 7944224012 scopus 로고    scopus 로고
    • Integrin β4 signaling promotes tumor angiogenesis
    • DOI 10.1016/j.ccr.2004.09.029, PII S1535610804002995
    • SN Nikolopoulos P Blaikie T Yoshioka W Guo FG Giancotti 2004 Integrin beta4 signaling promotes tumor angiogenesis Cancer Cell 6 471 483 10.1016/j.ccr.2004.09.029 1:CAS:528:DC%2BD2cXhtVGlurjM 15542431 (Pubitemid 39469983)
    • (2004) Cancer Cell , vol.6 , Issue.5 , pp. 471-483
    • Nikolopoulos, S.N.1    Blaikie, P.2    Yoshioka, T.3    Guo, W.4    Giancotti, F.G.5
  • 12
    • 77950257304 scopus 로고    scopus 로고
    • Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists
    • 10.1158/0008-5472.CAN-09-4032 1:CAS:528:DC%2BC3cXjtFygt70%3D 20197472
    • XH Yang LM Flores Q Li P Zhou F Xu IE Krop ME Hemler 2010 Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists Cancer Res 70 2256 2263 10.1158/0008-5472.CAN-09-4032 1:CAS:528:DC%2BC3cXjtFygt70%3D 20197472
    • (2010) Cancer Res , vol.70 , pp. 2256-2263
    • Yang, X.H.1    Flores, L.M.2    Li, Q.3    Zhou, P.4    Xu, F.5    Krop, I.E.6    Hemler, M.E.7
  • 15
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: More than meets the eye
    • F Berditchevski 2001 Complexes of tetraspanins with integrins: more than meets the eye J Cell Sci 114 4143 4151 1:CAS:528:DC%2BD3MXptlKrt7k%3D 11739647 (Pubitemid 33138652)
    • (2001) Journal of Cell Science , vol.114 , Issue.23 , pp. 4143-4151
    • Berditchevski, F.1
  • 16
    • 0037087710 scopus 로고    scopus 로고
    • Association of the tetraspanin CD151 with the laminin-binding integrins α3β1, α6Β1, α6β4 and α7β1 in cells in culture and in vivo
    • LM Sterk CA Geuijen JG van Den Berg N Claessen JJ Weening A Sonnenberg 2002 Association of the tetraspanin CD151 with the laminin-binding integrins alpha3beta1, alpha6beta1, alpha6beta4 and alpha7beta1 in cells in culture and in vivo J Cell Sci 115 1161 1173 1:CAS:528:DC%2BD38XivFGntr4%3D 11884516 (Pubitemid 34272481)
    • (2002) Journal of Cell Science , vol.115 , Issue.6 , pp. 1161-1173
    • Sterk, L.M.T.1    Geuijen, C.A.W.2    Van Den Berg, J.G.3    Claessen, N.4    Weening, J.J.5    Sonnenberg, A.6
  • 17
    • 0344708475 scopus 로고    scopus 로고
    • Tetraspanin Proteins Mediate Cellular Penetration, Invasion, and Fusion Events and Define a Novel Type of Membrane Microdomain
    • DOI 10.1146/annurev.cellbio.19.111301.153609
    • ME Hemler 2003 Tetraspanin proteins mediate cellular penetration, invasion and fusion events, and define a novel type of membrane microdomain Ann Rev Cell Dev Biol 19 397 422 10.1146/annurev.cellbio.19.111301.153609 1:CAS:528:DC%2BD3sXpsFamt7s%3D (Pubitemid 37487354)
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 397-422
    • Hemler, M.E.1
  • 18
    • 11244304502 scopus 로고    scopus 로고
    • Palmitoylation supports assembly and function of integrin-tetraspanin complexes
    • DOI 10.1083/jcb.200404100
    • X Yang OV Kovalenko W Tang C Claas CS Stipp ME Hemler 2004 Palmitoylation supports assembly and function of integrin-tetraspanin complexes J Cell Biol 167 1231 1240 10.1083/jcb.200404100 1:CAS:528:DC%2BD2MXmsVWm 15611341 (Pubitemid 40066636)
    • (2004) Journal of Cell Biology , vol.167 , Issue.6 , pp. 1231-1240
    • Yang, X.1    Kovalenko, O.V.2    Tang, W.3    Claas, C.4    Stipp, C.S.5    Hemler, M.E.6
  • 20
    • 33744826797 scopus 로고    scopus 로고
    • Protein palmitoylation by a family of DHHC protein S-acyltransferases
    • DOI 10.1194/jlr.R600007-JLR200
    • DA Mitchell A Vasudevan ME Linder RJ Deschenes 2006 Protein palmitoylation by a family of DHHC protein S-acyltransferases J Lipid Res 47 1118 1127 10.1194/jlr.R600007-JLR200 1:CAS:528:DC%2BD28XlvVeiu7k%3D 16582420 (Pubitemid 43830703)
    • (2006) Journal of Lipid Research , vol.47 , Issue.6 , pp. 1118-1127
    • Mitchell, D.A.1    Vasudevan, A.2    Linder, M.E.3    Deschenes, R.J.4
  • 21
    • 50049114778 scopus 로고    scopus 로고
    • Discovery of protein-palmitoylating enzymes
    • 10.1007/s00424-008-0465-x 1:CAS:528:DC%2BD1cXhtVSiurnL 18231805
    • R Tsutsumi Y Fukata M Fukata 2008 Discovery of protein-palmitoylating enzymes Pflugers Arch 456 1199 1206 10.1007/s00424-008-0465-x 1:CAS:528:DC%2BD1cXhtVSiurnL 18231805
    • (2008) Pflugers Arch , vol.456 , pp. 1199-1206
    • Tsutsumi, R.1    Fukata, Y.2    Fukata, M.3
  • 22
    • 33646830442 scopus 로고    scopus 로고
    • Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins
    • DOI 10.1016/j.bbalip.2006.03.010, PII S1388198106000709
    • Y Ohno A Kihara T Sano Y Igarashi 2006 Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins Biochim Biophys Acta 1761 474 483 1:CAS:528:DC%2BD28XltFGjt7w%3D 16647879 (Pubitemid 43776463)
    • (2006) Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids , vol.1761 , Issue.4 , pp. 474-483
    • Ohno, Y.1    Kihara, A.2    Sano, T.3    Igarashi, Y.4
  • 23
    • 33845451067 scopus 로고    scopus 로고
    • A receptors is required for normal assembly and function of GABAergic inhibitory synapses
    • DOI 10.1523/JNEUROSCI.4214-06.2006
    • C Fang L Deng CA Keller M Fukata Y Fukata G Chen B Luscher 2006 GODZ-mediated palmitoylation of GABA(A) receptors is required for normal assembly and function of GABAergic inhibitory synapses J Neurosci 26 12758 12768 10.1523/JNEUROSCI.4214-06.2006 1:CAS:528:DC%2BD2sXpslc%3D 17151279 (Pubitemid 44904571)
    • (2006) Journal of Neuroscience , vol.26 , Issue.49 , pp. 12758-12768
    • Fang, C.1    Deng, L.2    Keller, C.A.3    Fukata, M.4    Fukata, Y.5    Chen, G.6    Luscher, B.7
  • 24
    • 51049123096 scopus 로고    scopus 로고
    • DHHC2 affects palmitoylation and stability of tetraspanins CD9 and CD151
    • 10.1091/mbc.E07-11-1164 1:CAS:528:DC%2BD1cXpvV2hs7k%3D 18508921
    • C Sharma XH Yang ME Hemler 2008 DHHC2 affects palmitoylation and stability of tetraspanins CD9 and CD151 Mol Biol Cell 19 3415 3425 10.1091/mbc.E07-11-1164 1:CAS:528:DC%2BD1cXpvV2hs7k%3D 18508921
    • (2008) Mol Biol Cell , vol.19 , pp. 3415-3425
    • Sharma, C.1    Yang, X.H.2    Hemler, M.E.3
  • 26
    • 0025149021 scopus 로고
    • Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid
    • 1:CAS:528:DyaK3cXls12ntL8%3D 2398066
    • E Alvarez N Girones RJ Davis 1990 Inhibition of the receptor-mediated endocytosis of diferric transferrin is associated with the covalent modification of the transferrin receptor with palmitic acid J Biol Chem 265 16644 16655 1:CAS:528:DyaK3cXls12ntL8%3D 2398066
    • (1990) J Biol Chem , vol.265 , pp. 16644-16655
    • Alvarez, E.1    Girones, N.2    Davis, R.J.3
  • 27
    • 0035943686 scopus 로고    scopus 로고
    • Palmitoylation-dependent control of degradation, life span, and membrane expression of the CCR5 receptor
    • 10.1074/jbc.M104013200 1:CAS:528:DC%2BD3MXms1Smtr8%3D 11390405
    • Y Percherancier T Planchenault A Valenzuela-Fernandez JL Virelizier F Arenzana-Seisdedos F Bachelerie 2001 Palmitoylation-dependent control of degradation, life span, and membrane expression of the CCR5 receptor J Biol Chem 276 31936 31944 10.1074/jbc.M104013200 1:CAS:528:DC%2BD3MXms1Smtr8%3D 11390405
    • (2001) J Biol Chem , vol.276 , pp. 31936-31944
    • Percherancier, Y.1    Planchenault, T.2    Valenzuela-Fernandez, A.3    Virelizier, J.L.4    Arenzana-Seisdedos, F.5    Bachelerie, F.6
  • 28
    • 69549088095 scopus 로고    scopus 로고
    • Tetraspanin-enriched microdomains: A functional unit in cell plasma membranes
    • 10.1016/j.tcb.2009.06.004 1:CAS:528:DC%2BD1MXhtV2lu7zN 19709882
    • M Yanez-Mo O Barreiro M Gordon-Alonso M Sala-Valdes F Sanchez-Madrid 2009 Tetraspanin-enriched microdomains: a functional unit in cell plasma membranes Trends Cell Biol 19 434 446 10.1016/j.tcb.2009.06.004 1:CAS:528: DC%2BD1MXhtV2lu7zN 19709882
    • (2009) Trends Cell Biol , vol.19 , pp. 434-446
    • Yanez-Mo, M.1    Barreiro, O.2    Gordon-Alonso, M.3    Sala-Valdes, M.4    Sanchez-Madrid, F.5
  • 30
    • 0036198534 scopus 로고    scopus 로고
    • Palmitoylation of tetraspanin proteins: Modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology
    • DOI 10.1091/mbc.01-05-0275
    • X Yang C Claas SK Kraeft LB Chen Z Wang JA Kreidberg ME Hemler 2002 Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology Mol Biol Cell 13 767 781 10.1091/mbc.01-05-0275 1:CAS:528:DC%2BD38XivVeqtbY%3D 11907260 (Pubitemid 34250345)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.3 , pp. 767-781
    • Yang, X.1    Claas, C.2    Kraeft, S.-K.3    Chen, L.B.4    Wang, Z.5    Kreidberg, J.A.6    Hemler, M.E.7
  • 31
    • 0037020085 scopus 로고    scopus 로고
    • Expression of the palmitoylation-deficient CD151 weakens the association of alpha 3beta 1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signalling
    • 10.1074/jbc.M205265200 1:CAS:528:DC%2BD38XnsVaqt70%3D 12110679
    • F Berditchevski E Odintsova S Sawada E Gilbert 2002 Expression of the palmitoylation-deficient CD151 weakens the association of alpha 3beta 1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signalling J Biol Chem 277 36991 37000 10.1074/jbc.M205265200 1:CAS:528:DC%2BD38XnsVaqt70%3D 12110679
    • (2002) J Biol Chem , vol.277 , pp. 36991-37000
    • Berditchevski, F.1    Odintsova, E.2    Sawada, S.3    Gilbert, E.4
  • 32
    • 0037051906 scopus 로고    scopus 로고
    • Differential stability of tetraspanin/tetraspanin interactions: Role of palmitoylation
    • DOI 10.1016/S0014-5793(02)02522-X, PII S001457930202522X
    • S Charrin S Manie M Oualid M Billard C Boucheix E Rubinstein 2002 Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation FEBS Lett 516 139 144 10.1016/S0014-5793(02)02522-X 1:CAS:528:DC%2BD38XivVait7g%3D 11959120 (Pubitemid 34311950)
    • (2002) FEBS Letters , vol.516 , Issue.1-3 , pp. 139-144
    • Charrin, S.1    Manie, S.2    Oualid, M.3    Billard, M.4    Boucheix, C.5    Rubinstein, E.6
  • 34
    • 58249102251 scopus 로고    scopus 로고
    • Identification of G protein alpha subunit-palmitoylating enzyme
    • 10.1128/MCB.01144-08 1:CAS:528:DC%2BD1MXhsVChurY%3D 19001095
    • R Tsutsumi Y Fukata J Noritake T Iwanaga F Perez M Fukata 2009 Identification of G protein alpha subunit-palmitoylating enzyme Mol Cell Biol 29 435 447 10.1128/MCB.01144-08 1:CAS:528:DC%2BD1MXhsVChurY%3D 19001095
    • (2009) Mol Cell Biol , vol.29 , pp. 435-447
    • Tsutsumi, R.1    Fukata, Y.2    Noritake, J.3    Iwanaga, T.4    Perez, F.5    Fukata, M.6
  • 35
    • 78249258095 scopus 로고    scopus 로고
    • DHHC protein-dependent palmitoylation protects regulator of G-protein signaling 4 from proteasome degradation
    • 10.1016/j.febslet.2010.10.052 1:CAS:528:DC%2BC3cXhsVans7%2FM 21035448
    • J Wang Y Xie DW Wolff PW Abel Y Tu 2010 DHHC protein-dependent palmitoylation protects regulator of G-protein signaling 4 from proteasome degradation FEBS Lett 584 4570 4574 10.1016/j.febslet.2010.10.052 1:CAS:528:DC%2BC3cXhsVans7%2FM 21035448
    • (2010) FEBS Lett , vol.584 , pp. 4570-4574
    • Wang, J.1    Xie, Y.2    Wolff, D.W.3    Abel, P.W.4    Tu, Y.5
  • 36
    • 63049113014 scopus 로고    scopus 로고
    • Phosphorylation of a novel site on the {beta}4 integrin at the trailing edge of migrating cells promotes hemidesmosome disassembly
    • 10.1091/mbc.E08-06-0646 1:CAS:528:DC%2BD1MXht1Sktbg%3D 19005215
    • EC Germain TM Santos I Rabinovitz 2009 Phosphorylation of a novel site on the {beta}4 integrin at the trailing edge of migrating cells promotes hemidesmosome disassembly Mol Biol Cell 20 56 67 10.1091/mbc.E08-06-0646 1:CAS:528:DC%2BD1MXht1Sktbg%3D 19005215
    • (2009) Mol Biol Cell , vol.20 , pp. 56-67
    • Germain, E.C.1    Santos, T.M.2    Rabinovitz, I.3
  • 37
    • 80053355409 scopus 로고    scopus 로고
    • Role of β4 integrin phosphorylation in human invasive squamous cell carcinoma: Regulation of hemidesmosome stability modulates cell migration
    • 10.1038/labinvest.2011.104 1:CAS:528:DC%2BC3MXht1Ghu7zP 21769085
    • T Kashyap E Germain M Roche S Lyle I Rabinovitz 2011 Role of β4 integrin phosphorylation in human invasive squamous cell carcinoma: regulation of hemidesmosome stability modulates cell migration Lab Invest 91 1414 1426 10.1038/labinvest.2011.104 1:CAS:528:DC%2BC3MXht1Ghu7zP 21769085
    • (2011) Lab Invest , vol.91 , pp. 1414-1426
    • Kashyap, T.1    Germain, E.2    Roche, M.3    Lyle, S.4    Rabinovitz, I.5
  • 38
    • 33746587831 scopus 로고    scopus 로고
    • Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase
    • DOI 10.1083/jcb.200601051
    • C Fernandez-Hernando M Fukata PN Bernatchez Y Fukata MI Lin DS Bredt WC Sessa 2006 Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase J Cell Biol 174 369 377 10.1083/jcb.200601051 1:CAS:528:DC%2BD28XnvF2htrY%3D 16864653 (Pubitemid 44156767)
    • (2006) Journal of Cell Biology , vol.174 , Issue.3 , pp. 369-377
    • Fernandez-Hernando, C.1    Fukata, M.2    Bernatchez, P.N.3    Fukata, Y.4    Lin, M.I.5    Bredt, D.S.6    Sessa, W.C.7
  • 39
    • 0036151461 scopus 로고    scopus 로고
    • Function of the tetraspanin CD151-α6β1 integrin complex during cellular morphogenesis
    • DOI 10.1091/mbc.01-10-0481
    • XA Zhang AR Kazarov X Yang AL Bontrager CS Stipp ME Hemler 2002 Function of the tetraspanin CD151-alpha6beta1 integrin complex during cellular morphogenesis Mol Biol Cell 13 1 11 10.1091/mbc.01-10-0481 11809818 (Pubitemid 34106054)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.1 , pp. 1-11
    • Zhang, X.A.1    Kazarov, A.R.2    Yang, X.3    Bontrager, A.L.4    Stipp, C.S.5    Hemler, M.E.6
  • 40
    • 34548477663 scopus 로고    scopus 로고
    • Serine phosphorylation of the integrin β4 subunit is necessary for epidermal growth factor receptor-induced hemidesmosome disruption
    • DOI 10.1091/mbc.E07-04-0306
    • K Wilhelmsen SH Litjens I Kuikman C Margadant J van Rheenen A Sonnenberg 2007 Serine phosphorylation of the integrin beta4 subunit is necessary for epidermal growth factor receptor induced hemidesmosome disruption Mol Biol Cell 18 3512 3522 10.1091/mbc.E07-04-0306 1:CAS:528:DC%2BD2sXhtVWnt7bK 17615294 (Pubitemid 47378689)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.9 , pp. 3512-3522
    • Wilhelmsen, K.1    Litjens, S.H.M.2    Kuikman, I.3    Margadant, C.4    Van Rheenen, J.5    Sonnenberg, A.6
  • 41
    • 54049132555 scopus 로고    scopus 로고
    • Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein
    • 10.1074/jbc.M802140200 1:CAS:528:DC%2BD1cXhtVGktbbN 18596047
    • J Greaves C Salaun Y Fukata M Fukata LH Chamberlain 2008 Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein J Biol Chem 283 25014 25026 10.1074/jbc.M802140200 1:CAS:528: DC%2BD1cXhtVGktbbN 18596047
    • (2008) J Biol Chem , vol.283 , pp. 25014-25026
    • Greaves, J.1    Salaun, C.2    Fukata, Y.3    Fukata, M.4    Chamberlain, L.H.5
  • 42
    • 79955649200 scopus 로고    scopus 로고
    • DHHC palmitoyl transferases: Substrate interactions and (patho)physiology
    • 10.1016/j.tibs.2011.01.003 1:CAS:528:DC%2BC3MXmtFCrt78%3D 21388813
    • J Greaves LH Chamberlain 2011 DHHC palmitoyl transferases: substrate interactions and (patho)physiology Trends Biochem Sci 36 245 253 10.1016/j.tibs.2011.01.003 1:CAS:528:DC%2BC3MXmtFCrt78%3D 21388813
    • (2011) Trends Biochem Sci , vol.36 , pp. 245-253
    • Greaves, J.1    Chamberlain, L.H.2
  • 43
    • 0028840521 scopus 로고
    • Between molecules and morphology. Extracellular matrix and creation of vascular form
    • 1:STN:280:DyaK28%2FhtVamsA%3D%3D 7573362
    • RB Vernon EH Sage 1995 Between molecules and morphology. Extracellular matrix and creation of vascular form Am J Pathol 147 873 883 1:STN:280:DyaK28%2FhtVamsA%3D%3D 7573362
    • (1995) Am J Pathol , vol.147 , pp. 873-883
    • Vernon, R.B.1    Sage, E.H.2
  • 44
    • 0028954485 scopus 로고
    • Regulation of endothelial cell morphogenesis by integrins, mechanical forces, and matrix guidance pathways
    • 10.1006/excr.1995.1015 1:CAS:528:DyaK2MXjtVersLg%3D 7813611
    • GE Davis CW Camarillo 1995 Regulation of endothelial cell morphogenesis by integrins, mechanical forces, and matrix guidance pathways Exp Cell Res 216 113 123 10.1006/excr.1995.1015 1:CAS:528:DyaK2MXjtVersLg%3D 7813611
    • (1995) Exp Cell Res , vol.216 , pp. 113-123
    • Davis, G.E.1    Camarillo, C.W.2
  • 45
    • 72449200272 scopus 로고    scopus 로고
    • Integrin (alpha6beta4) signals through Src to increase expression of S100A4, a metastasis-promoting factor: Implications for cancer cell invasion
    • 10.1158/1541-7786.MCR-09-0102 1:CAS:528:DC%2BD1MXhtlSqs7nL 19808905
    • TH Kim HI Kim YH Soung LA Shaw J Chung 2009 Integrin (alpha6beta4) signals through Src to increase expression of S100A4, a metastasis-promoting factor: implications for cancer cell invasion Mol Cancer Res 7 1605 1612 10.1158/1541-7786.MCR-09-0102 1:CAS:528:DC%2BD1MXhtlSqs7nL 19808905
    • (2009) Mol Cancer Res , vol.7 , pp. 1605-1612
    • Kim, T.H.1    Kim, H.I.2    Soung, Y.H.3    Shaw, L.A.4    Chung, J.5
  • 47
    • 65649108966 scopus 로고    scopus 로고
    • The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases
    • 10.1091/mbc.E08-09-0944 1:CAS:528:DC%2BD1MXlsFygsrc%3D 19158383
    • J Greaves GR Prescott Y Fukata M Fukata C Salaun LH Chamberlain 2009 The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases Mol Biol Cell 20 1845 1854 10.1091/mbc.E08-09-0944 1:CAS:528:DC%2BD1MXlsFygsrc%3D 19158383
    • (2009) Mol Biol Cell , vol.20 , pp. 1845-1854
    • Greaves, J.1    Prescott, G.R.2    Fukata, Y.3    Fukata, M.4    Salaun, C.5    Chamberlain, L.H.6
  • 48
    • 0018661114 scopus 로고
    • Cathepsin D: The lysosomal aspartic proteinase
    • Barrett AJ (1979) Cathepsin D: the lysosomal aspartic proteinase. Ciba Found Symp, pp 37-50
    • (1979) Ciba Found Symp , pp. 37-50
    • Barrett, A.J.1
  • 49
    • 0023943263 scopus 로고
    • Cathepsin D is membrane-associated in macrophage endosomes
    • 1:CAS:528:DyaL1cXktVartLw%3D 3360812
    • S Diment MS Leech PD Stahl 1988 Cathepsin D is membrane-associated in macrophage endosomes J Biol Chem 263 6901 6907 1:CAS:528:DyaL1cXktVartLw%3D 3360812
    • (1988) J Biol Chem , vol.263 , pp. 6901-6907
    • Diment, S.1    Leech, M.S.2    Stahl, P.D.3
  • 50
    • 0029160297 scopus 로고
    • Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump
    • 10.1083/jcb.130.4.821 7642700
    • AW van Weert KW Dunn HJ Gueze FR Maxfield W Stoorvogel 1995 Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump J Cell Biol 130 821 834 10.1083/jcb.130.4.821 7642700
    • (1995) J Cell Biol , vol.130 , pp. 821-834
    • Van Weert, A.W.1    Dunn, K.W.2    Gueze, H.J.3    Maxfield, F.R.4    Stoorvogel, W.5
  • 51
    • 65249142254 scopus 로고    scopus 로고
    • Tetraspanin proteins regulate membrane type-1 matrix metalloproteinase- dependent pericellular proteolysis
    • 10.1091/mbc.E08-11-1149 1:CAS:528:DC%2BD1MXotVyqsLo%3D 19211836
    • MA Lafleur D Xu ME Hemler 2009 Tetraspanin proteins regulate membrane type-1 matrix metalloproteinase-dependent pericellular proteolysis Mol Biol Cell 20 2030 2040 10.1091/mbc.E08-11-1149 1:CAS:528:DC%2BD1MXotVyqsLo%3D 19211836
    • (2009) Mol Biol Cell , vol.20 , pp. 2030-2040
    • Lafleur, M.A.1    Xu, D.2    Hemler, M.E.3
  • 52
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: Policing protein stability and traffic
    • DOI 10.1038/nrm2084, PII NRM2084
    • ME Linder RJ Deschenes 2007 Palmitoylation: policing protein stability and traffic Natl Rev Mol Cell Biol 8 74 84 10.1038/nrm2084 1:CAS:528: DC%2BD28XhtlCjt7bL (Pubitemid 46012016)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.1 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 54
    • 80054716502 scopus 로고    scopus 로고
    • Protein palmitoylation and subcellular trafficking
    • 10.1016/j.bbamem.2011.07.009 1:CAS:528:DC%2BC3MXhtlejt7rN 21819967
    • C Aicart-Ramos RA Valero I Rodriguez-Crespo 2011 Protein palmitoylation and subcellular trafficking Biochim Biophys Acta 1808 2981 2994 10.1016/j.bbamem.2011.07.009 1:CAS:528:DC%2BC3MXhtlejt7rN 21819967
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 2981-2994
    • Aicart-Ramos, C.1    Valero, R.A.2    Rodriguez-Crespo, I.3


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