메뉴 건너뛰기




Volumn 1833, Issue 8, 2013, Pages 1876-1884

The role of MPP1/p55 and its palmitoylation in resting state raft organization in HEL cells

Author keywords

Erythroid HEL cells; FLIM technique; Membrane rafts; MPP1 silencing; MPP1 p55; Palmitoylation

Indexed keywords

TYROSINE KINASE RECEPTOR;

EID: 84877839154     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.03.009     Document Type: Article
Times cited : (24)

References (54)
  • 1
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: a report on the Keystone Symposium on Lipid Rafts and Cell Function
    • Pike L.J. Rafts defined: a report on the Keystone Symposium on Lipid Rafts and Cell Function. J. Lipid Res. 2006, 47:1597-1598.
    • (2006) J. Lipid Res. , vol.47 , pp. 1597-1598
    • Pike, L.J.1
  • 2
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: contentious only from simplistic standpoints
    • Hancock J.F. Lipid rafts: contentious only from simplistic standpoints. Nat. Rev. Mol. Cell Biol. 2006, 7:456-462.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 456-462
    • Hancock, J.F.1
  • 3
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: new tools and insights
    • Simons K., Gerl M.J. Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 2010, 11:688-699.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 4
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D., Simons K. Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 7
    • 84857737571 scopus 로고    scopus 로고
    • DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities
    • Jennings B.C., Linder M.E. DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities. J. Biol. Chem. 2012, 287:7236-7245.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7236-7245
    • Jennings, B.C.1    Linder, M.E.2
  • 9
    • 61449149636 scopus 로고    scopus 로고
    • Palmitoylation cycles and regulation of protein function (review)
    • Baekkeskov S., Kanaani J. Palmitoylation cycles and regulation of protein function (review). Mol. Membr. Biol. 2009, 26:42-54.
    • (2009) Mol. Membr. Biol. , vol.26 , pp. 42-54
    • Baekkeskov, S.1    Kanaani, J.2
  • 10
    • 34247590130 scopus 로고    scopus 로고
    • Palmitoylation of ligands, receptors, and intracellular signaling molecules
    • Resh M.D. Palmitoylation of ligands, receptors, and intracellular signaling molecules. Sci. STKE 2006, 2006:re14.
    • (2006) Sci. STKE , vol.2006
    • Resh, M.D.1
  • 11
  • 12
    • 0034682847 scopus 로고    scopus 로고
    • Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae
    • Uittenbogaard A., Smart E.J. Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae. J. Biol. Chem. 2000, 275:25595-25599.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25595-25599
    • Uittenbogaard, A.1    Smart, E.J.2
  • 13
    • 0032561327 scopus 로고    scopus 로고
    • Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues
    • Arni S., Keilbaugh S.A., Ostermeyer A.G., Brown D.A. Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues. J. Biol. Chem. 1998, 273:28478-28485.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28478-28485
    • Arni, S.1    Keilbaugh, S.A.2    Ostermeyer, A.G.3    Brown, D.A.4
  • 14
    • 0037438349 scopus 로고    scopus 로고
    • Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling
    • Fragoso R., Ren D., Zhang X., Su M.W., Burakoff S.J., Jin Y.J. Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling. J. Immunol. 2003, 170:913-921.
    • (2003) J. Immunol. , vol.170 , pp. 913-921
    • Fragoso, R.1    Ren, D.2    Zhang, X.3    Su, M.W.4    Burakoff, S.J.5    Jin, Y.J.6
  • 15
    • 21444450396 scopus 로고    scopus 로고
    • Palmitoylation and intracellular domain interactions both contribute to raft targeting of linker for activation of T cells
    • Shogomori H., Hammond A.T., Ostermeyer-Fay A.G., Barr D.J., Feigenson G.W., London E., Brown D.A. Palmitoylation and intracellular domain interactions both contribute to raft targeting of linker for activation of T cells. J. Biol. Chem. 2005, 280:18931-18942.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18931-18942
    • Shogomori, H.1    Hammond, A.T.2    Ostermeyer-Fay, A.G.3    Barr, D.J.4    Feigenson, G.W.5    London, E.6    Brown, D.A.7
  • 16
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang W., Trible R.P., Samelson L.E. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 1998, 9:239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 17
    • 77955033375 scopus 로고    scopus 로고
    • Greasing their way: lipid modifications determine protein association with membrane rafts
    • Levental I., Grzybek M., Simons K. Greasing their way: lipid modifications determine protein association with membrane rafts. Biochemistry 2010, 49:6305-6316.
    • (2010) Biochemistry , vol.49 , pp. 6305-6316
    • Levental, I.1    Grzybek, M.2    Simons, K.3
  • 20
    • 0025994663 scopus 로고
    • Molecular identification of a major palmitoylated erythrocyte membrane protein containing the src homology 3 motif
    • Ruff P., Speicher D.W., Husain-Chishti A. Molecular identification of a major palmitoylated erythrocyte membrane protein containing the src homology 3 motif. Proc. Natl. Acad. Sci. U. S. A. 1991, 88:6595-6599.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 6595-6599
    • Ruff, P.1    Speicher, D.W.2    Husain-Chishti, A.3
  • 21
    • 0029851093 scopus 로고    scopus 로고
    • Modular organization of the PDZ domains in the human discs-large protein suggests a mechanism for coupling PDZ domain-binding proteins to ATP and the membrane cytoskeleton
    • Marfatia S.M., Morais Cabral J.H., Lin L., Hough C., Bryant P.J., Stolz L., Chishti A.H. Modular organization of the PDZ domains in the human discs-large protein suggests a mechanism for coupling PDZ domain-binding proteins to ATP and the membrane cytoskeleton. J. Cell Biol. 1996, 135:753-766.
    • (1996) J. Cell Biol. , vol.135 , pp. 753-766
    • Marfatia, S.M.1    Morais Cabral, J.H.2    Lin, L.3    Hough, C.4    Bryant, P.J.5    Stolz, L.6    Chishti, A.H.7
  • 22
    • 0028944110 scopus 로고
    • Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte
    • Hemming N.J., Anstee D.J., Staricoff M.A., Tanner M.J., Mohandas N. Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte. J. Biol. Chem. 1995, 270:5360-5366.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5360-5366
    • Hemming, N.J.1    Anstee, D.J.2    Staricoff, M.A.3    Tanner, M.J.4    Mohandas, N.5
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 1979, 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 26
    • 33748958993 scopus 로고    scopus 로고
    • Use of analogs and inhibitors to study the functional significance protein palmitoylation
    • Resh M.D. Use of analogs and inhibitors to study the functional significance protein palmitoylation. Methods 2006, 40:191-197.
    • (2006) Methods , vol.40 , pp. 191-197
    • Resh, M.D.1
  • 27
    • 38449114971 scopus 로고    scopus 로고
    • Detergent resistance as a tool in membrane research
    • Lingwood D., Simons K. Detergent resistance as a tool in membrane research. Nat. Protoc. 2007, 2:2159-2165.
    • (2007) Nat. Protoc. , vol.2 , pp. 2159-2165
    • Lingwood, D.1    Simons, K.2
  • 28
    • 33744941819 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging provides enhanced contrast when imaging the phase-sensitive dye di-4-ANEPPDHQ in model membranes and live cells
    • Owen D.M., Lanigan P.M., Dunsby C., Munro I., Grant D., Neil M.A., French P.M., Magee A.I. Fluorescence lifetime imaging provides enhanced contrast when imaging the phase-sensitive dye di-4-ANEPPDHQ in model membranes and live cells. Biophys. J. 2006, 90:L80-L82.
    • (2006) Biophys. J. , vol.90
    • Owen, D.M.1    Lanigan, P.M.2    Dunsby, C.3    Munro, I.4    Grant, D.5    Neil, M.A.6    French, P.M.7    Magee, A.I.8
  • 30
    • 60549110938 scopus 로고    scopus 로고
    • Lipid rafts and caveolae in signaling by growth factor receptors
    • de Laurentiis A., Donovan L., Arcaro A. Lipid rafts and caveolae in signaling by growth factor receptors. Open Biochem. J. 2007, 1:12-32.
    • (2007) Open Biochem. J. , vol.1 , pp. 12-32
    • de Laurentiis, A.1    Donovan, L.2    Arcaro, A.3
  • 31
    • 33747613351 scopus 로고    scopus 로고
    • Cytokine signals modulated via lipid rafts mimic niche signals and induce hibernation in hematopoietic stem cells
    • Yamazaki S., Iwama A., Takayanagi S., Morita Y., Eto K., Ema H., Nakauchi H. Cytokine signals modulated via lipid rafts mimic niche signals and induce hibernation in hematopoietic stem cells. EMBO J. 2006, 25:3515-3523.
    • (2006) EMBO J. , vol.25 , pp. 3515-3523
    • Yamazaki, S.1    Iwama, A.2    Takayanagi, S.3    Morita, Y.4    Eto, K.5    Ema, H.6    Nakauchi, H.7
  • 36
    • 2442494090 scopus 로고    scopus 로고
    • CD4 raft association and signaling regulate molecular clustering at the immunological synapse site
    • Balamuth F., Brogdon J.L., Bottomly K. CD4 raft association and signaling regulate molecular clustering at the immunological synapse site. J. Immunol. 2004, 172:5887-5892.
    • (2004) J. Immunol. , vol.172 , pp. 5887-5892
    • Balamuth, F.1    Brogdon, J.L.2    Bottomly, K.3
  • 37
    • 0034614557 scopus 로고    scopus 로고
    • Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids
    • Webb Y., Hermida-Matsumoto L., Resh M.D. Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids. J. Biol. Chem. 2000, 275:261-270.
    • (2000) J. Biol. Chem. , vol.275 , pp. 261-270
    • Webb, Y.1    Hermida-Matsumoto, L.2    Resh, M.D.3
  • 38
    • 0034695484 scopus 로고    scopus 로고
    • Lipid-dependent targeting of G proteins into rafts
    • Moffett S., Brown D.A., Linder M.E. Lipid-dependent targeting of G proteins into rafts. J. Biol. Chem. 2000, 275:2191-2198.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2191-2198
    • Moffett, S.1    Brown, D.A.2    Linder, M.E.3
  • 39
    • 78650664669 scopus 로고    scopus 로고
    • Palmitoylation regulates raft affinity for the majority of integral raft proteins
    • Levental I., Lingwood D., Grzybek M., Coskun U., Simons K. Palmitoylation regulates raft affinity for the majority of integral raft proteins. Proc. Natl. Acad. Sci. U. S. A. 2010, 107(51):22050-22054.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.51 , pp. 22050-22054
    • Levental, I.1    Lingwood, D.2    Grzybek, M.3    Coskun, U.4    Simons, K.5
  • 40
    • 84864075435 scopus 로고    scopus 로고
    • RNAiAtlas: a database for RNAi (siRNA) libraries and their specificity
    • bas027
    • Mazur S., Csucs G., Kozak K. RNAiAtlas: a database for RNAi (siRNA) libraries and their specificity. Database (Oxford) 2012, 2012:bas027.
    • (2012) Database (Oxford) , vol.2012
    • Mazur, S.1    Csucs, G.2    Kozak, K.3
  • 41
    • 84877796935 scopus 로고    scopus 로고
    • http://hcdc.ethz.ch/index.php?view=article&id=25.
  • 42
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • Lichtenberg D., Goni F.M., Heerklotz H. Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem. Sci. 2005, 30:430-436.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 430-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 43
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells
    • Glebov O.O., Bright N.A., Nichols B.J. Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells. Nat. Cell Biol. 2006, 8:46-54.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 44
    • 77951895530 scopus 로고    scopus 로고
    • Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins
    • Fujita M., Kinoshita T. Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins. FEBS Lett. 2010, 584:1670-1677.
    • (2010) FEBS Lett. , vol.584 , pp. 1670-1677
    • Fujita, M.1    Kinoshita, T.2
  • 45
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: scale-dependent, active lipid organization at the cell surface
    • Mayor S., Rao M. Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 2004, 5:231-240.
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 48
    • 0037020085 scopus 로고    scopus 로고
    • Expression of the palmitoylation-deficient CD151 weakens the association of alpha 3 beta 1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling
    • Berditchevski F., Odintsova E., Sawada S., Gilbert E. Expression of the palmitoylation-deficient CD151 weakens the association of alpha 3 beta 1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling. J. Biol. Chem. 2002, 277:36991-37000.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36991-37000
    • Berditchevski, F.1    Odintsova, E.2    Sawada, S.3    Gilbert, E.4
  • 49
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler M.E. Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell Biol. 2005, 6:801-811.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 50
    • 2942674545 scopus 로고    scopus 로고
    • Palmitoylation regulates the clustering and cell surface stability of GABAA receptors
    • Rathenberg J., Kittler J.T., Moss S.J. Palmitoylation regulates the clustering and cell surface stability of GABAA receptors. Mol. Cell. Neurosci. 2004, 26:251-257.
    • (2004) Mol. Cell. Neurosci. , vol.26 , pp. 251-257
    • Rathenberg, J.1    Kittler, J.T.2    Moss, S.J.3
  • 51
    • 33846247103 scopus 로고    scopus 로고
    • Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling
    • Feig C., Tchikov V., Schutze S., Peter M.E. Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling. EMBO J. 2007, 26:221-231.
    • (2007) EMBO J. , vol.26 , pp. 221-231
    • Feig, C.1    Tchikov, V.2    Schutze, S.3    Peter, M.E.4
  • 52
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • Anderson R.G., Jacobson K. A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains. Science 2002, 296:1821-1825.
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.1    Jacobson, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.