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Volumn 31, Issue 2, 2003, Pages 556-561

Cellular uptake of Antennapedia Penetratin peptides is a two-step process in which phase transfer precedes a tryptophan-dependent translocation

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HOMEODOMAIN PROTEIN; MEMBRANE LIPID; MUTANT PROTEIN; OLIGONUCLEOTIDE; PHENYLALANINE; TRYPTOPHAN;

EID: 0037440187     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg160     Document Type: Review
Times cited : (125)

References (33)
  • 1
    • 0033957805 scopus 로고    scopus 로고
    • The homeodomain resource: A prototype database for a large protein family
    • Banerjee-Basu,S., Ryan,J.F. and Baxevanis,A.D. (2000) The homeodomain resource: a prototype database for a large protein family. Nucleic Acids Res., 28, 329-330.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 329-330
    • Banerjee-Basu, S.1    Ryan, J.F.2    Baxevanis, A.D.3
  • 4
    • 0033582545 scopus 로고    scopus 로고
    • Structure of a HoxB1-Pbx1 heterodimer bound to DNA: Role of the hexapeptide and a fourth homeodomain helix in complex formation
    • Piper,D.E., Batchelor,A.H., Chang,C.P., Cleary,M.L. and Wolberger,C. (1999) Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation. Cell, 96, 587-597.
    • (1999) Cell , vol.96 , pp. 587-597
    • Piper, D.E.1    Batchelor, A.H.2    Chang, C.P.3    Cleary, M.L.4    Wolberger, C.5
  • 5
    • 0033602242 scopus 로고    scopus 로고
    • Structure of a DNA-bound Ultrabithorax-Extradenticle homeodomain complex
    • Passner,J.M., Ryoo,H.D., Shen,L., Mann,R.S. and Aggarwal,A.K. (1999) Structure of a DNA-bound Ultrabithorax-Extradenticle homeodomain complex. Nature, 397, 714-719.
    • (1999) Nature , vol.397 , pp. 714-719
    • Passner, J.M.1    Ryoo, H.D.2    Shen, L.3    Mann, R.S.4    Aggarwal, A.K.5
  • 6
    • 0033853989 scopus 로고    scopus 로고
    • Homeodomain position 54 specifies transcriptional versus translational control by Bicoid
    • Niessing,D., Driever,W., Sprenger,F., Taubert,H., Jackle,H. and Rivera-Pomar,R. (2000) Homeodomain position 54 specifies transcriptional versus translational control by Bicoid. Mol. Cell., 5, 395-401.
    • (2000) Mol. Cell. , vol.5 , pp. 395-401
    • Niessing, D.1    Driever, W.2    Sprenger, F.3    Taubert, H.4    Jackle, H.5    Rivera-Pomar, R.6
  • 7
    • 0345898928 scopus 로고    scopus 로고
    • Homeodomain-interacting protein kinases, a novel family of corepressors for homeodomain transcription factors
    • Kim,Y.H., Choi,C.Y., Lee,S.J., Conti,M.A. and Kim,Y. (1998) Homeodomain-interacting protein kinases, a novel family of corepressors for homeodomain transcription factors. J. Biol. Chem., 273, 25875-25879.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25875-25879
    • Kim, Y.H.1    Choi, C.Y.2    Lee, S.J.3    Conti, M.A.4    Kim, Y.5
  • 8
    • 0033962883 scopus 로고    scopus 로고
    • The homeodomain of PDX-1 mediates multiple protein-protein interactions in the formation of a transcriptional activation complex on the insulin promoter
    • Ohneda,K., Mirmira,R.G., Wang,J., Johnson,J.D. and German,M.S. (2000) The homeodomain of PDX-1 mediates multiple protein-protein interactions in the formation of a transcriptional activation complex on the insulin promoter. Mol. Cell. Biol., 20, 900-911.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 900-911
    • Ohneda, K.1    Mirmira, R.G.2    Wang, J.3    Johnson, J.D.4    German, M.S.5
  • 9
    • 0029811475 scopus 로고    scopus 로고
    • HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation
    • Zappavigna,V., Falciola,L., Helmer-Citterich,M., Mavilio,F. and Bianchi,M.E. (1996) HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation. EMBO J., 15, 4981-4991.
    • (1996) EMBO J. , vol.15 , pp. 4981-4991
    • Zappavigna, V.1    Falciola, L.2    Helmer-Citterich, M.3    Mavilio, F.4    Bianchi, M.E.5
  • 10
    • 0028350269 scopus 로고
    • Specificity of HOX protein function depends on DNA-protein and protein-protein interactions, both mediated by the homeo domain
    • Zappavigna,V., Sartori,D. and Mavilio,F. (1994) Specificity of HOX protein function depends on DNA-protein and protein-protein interactions, both mediated by the homeo domain. Genes Dev., 8, 732-744.
    • (1994) Genes Dev. , vol.8 , pp. 732-744
    • Zappavigna, V.1    Sartori, D.2    Mavilio, F.3
  • 12
    • 0029944653 scopus 로고    scopus 로고
    • A role for the Msx-1 homeodomain in transcriptional regulation: Residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional repression
    • Zhang,H., Catron,K.M. and Abate-Shen,C. (1996). A role for the Msx-1 homeodomain in transcriptional regulation: residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional repression. Proc. Natl Acad. Sci. USA, 93, 1764-1769.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1764-1769
    • Zhang, H.1    Catron, K.M.2    Abate-Shen, C.3
  • 13
    • 0029894663 scopus 로고    scopus 로고
    • Repression by HoxA7 is mediated by the homeodomain and the modulatory action of its N-terminal-arm residues
    • Schnabel,C.A. and Abate-Shen,C. (1996) Repression by HoxA7 is mediated by the homeodomain and the modulatory action of its N-terminal-arm residues. Mol. Cell. Biol., 16, 2678-2688.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2678-2688
    • Schnabel, C.A.1    Abate-Shen, C.2
  • 14
    • 0029862814 scopus 로고    scopus 로고
    • Three distinct domains in the HOX-11 homeobox oncoprotein are required for optimal transactivation
    • Zhang,N., Shen,W., Ho,A.D. and Lu,M. (1996) Three distinct domains in the HOX-11 homeobox oncoprotein are required for optimal transactivation. Oncogene, 13, 1781-1787.
    • (1996) Oncogene , vol.13 , pp. 1781-1787
    • Zhang, N.1    Shen, W.2    Ho, A.D.3    Lu, M.4
  • 15
    • 0033521623 scopus 로고    scopus 로고
    • Activity regulation of a Hox protein and a role for the homeodomain in inhibiting transcriptional activation
    • Li,X., Murre,C. and McGinnis,W. (1999) Activity regulation of a Hox protein and a role for the homeodomain in inhibiting transcriptional activation. EMBO J., 18, 198-211.
    • (1999) EMBO J. , vol.18 , pp. 198-211
    • Li, X.1    Murre, C.2    McGinnis, W.3
  • 16
    • 0030273590 scopus 로고    scopus 로고
    • Getting hydrophilic compounds into cells: Lessons from homeopeptides
    • Prochiantz,A. (1996) Getting hydrophilic compounds into cells: lessons from homeopeptides. Curr. Opin. Neurobiol., 6, 629-634.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 629-634
    • Prochiantz, A.1
  • 17
    • 0033948268 scopus 로고    scopus 로고
    • Messenger proteins: Homeoproteins, TAT and others
    • Prochiantz,A. (2000) Messenger proteins: homeoproteins, TAT and others. Curr. Opin. Cell Biol., 12, 400-406.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 400-406
    • Prochiantz, A.1
  • 18
    • 0027424656 scopus 로고
    • Neurotrophic activity of the Antennapedia homeodomain depends on its specific DNA-binding properties
    • LeRoux,I., Joliot,A.H., Bloch-Gallego,E., Prochiantz,A. and Volovitch,M. (1993) Neurotrophic activity of the Antennapedia homeodomain depends on its specific DNA-binding properties. Proc. Natl Acad. Sci. USA, 90, 9120-9124.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9120-9124
    • LeRoux, I.1    Joliot, A.H.2    Bloch-Gallego, E.3    Prochiantz, A.4    Volovitch, M.5
  • 19
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi,D., Joliot,A.H., Chassaing,G. and Prochiantz,A. (1994) The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem., 269, 10444-10450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 20
    • 0032537741 scopus 로고    scopus 로고
    • Identification of a signal sequence necessary for the unconventional secretion of Engrailed homeoprotein
    • Joliot,A., Maizel,A., Rosenberg,D., Trembleau,A., Dupas,S., Volovitch,M. and Prochiantz,A. (1998) Identification of a signal sequence necessary for the unconventional secretion of Engrailed homeoprotein. Curr. Biol., 8, 856-863.
    • (1998) Curr. Biol. , vol.8 , pp. 856-863
    • Joliot, A.1    Maizel, A.2    Rosenberg, D.3    Trembleau, A.4    Dupas, S.5    Volovitch, M.6    Prochiantz, A.7
  • 21
    • 0032813156 scopus 로고    scopus 로고
    • A short region of its homeodomain is necessary for engrailed nuclear export and secretion
    • Maizel,A., Bensaude,O., Prochiantz,A. and Joliot,A. (1999) A short region of its homeodomain is necessary for engrailed nuclear export and secretion. Development, 126, 3183-3190.
    • (1999) Development , vol.126 , pp. 3183-3190
    • Maizel, A.1    Bensaude, O.2    Prochiantz, A.3    Joliot, A.4
  • 22
    • 0029923186 scopus 로고    scopus 로고
    • Transcription factor hoxa-5 is taken up by cells in culture and conveyed to their nuclei
    • Chatelin,L., Volovitch,M., Joliot,A.H., Perez,F. and Prochiantz,A. (1996) Transcription factor hoxa-5 is taken up by cells in culture and conveyed to their nuclei. Mech. Dev., 55, 111-117.
    • (1996) Mech. Dev. , vol.55 , pp. 111-117
    • Chatelin, L.1    Volovitch, M.2    Joliot, A.H.3    Perez, F.4    Prochiantz, A.5
  • 23
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi,D., Calvet,S., Trembleau,A., Brunissen,A., Chassaing,G. and Prochiantz,A. (1996) Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem., 271, 18188-18193.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 24
    • 0029802678 scopus 로고    scopus 로고
    • Conformational and associative behaviours of the third helix of antennapedia homeodomain in membrane-mimetic environments
    • Berlose,J.P., Convert,O., Derossi,D., Brunissen,A. and Chassaing,G. (1996) Conformational and associative behaviours of the third helix of antennapedia homeodomain in membrane-mimetic environments. Eur. J. Biochem., 242, 372-386.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 372-386
    • Berlose, J.P.1    Convert, O.2    Derossi, D.3    Brunissen, A.4    Chassaing, G.5
  • 25
    • 0035078052 scopus 로고    scopus 로고
    • Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity
    • Drin,G., Mazel,M., Clair,P., Mathieu,D., Kaczorek,M. and Temsamani,J. (2001) Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity. Eur. J. Biochem., 268, 1304-1314.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1304-1314
    • Drin, G.1    Mazel, M.2    Clair, P.3    Mathieu, D.4    Kaczorek, M.5    Temsamani, J.6
  • 26
    • 0033802715 scopus 로고    scopus 로고
    • Evidence for an amphipathicity independent cellular uptake of amphipathic cell-penetrating peptides
    • Scheller,A., Wiesner,B., Melzig,M., Bienert,M. and Oehlke,J. (2000) Evidence for an amphipathicity independent cellular uptake of amphipathic cell-penetrating peptides. Eur. J. Biochem., 267, 6043-6050.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6043-6050
    • Scheller, A.1    Wiesner, B.2    Melzig, M.3    Bienert, M.4    Oehlke, J.5
  • 28
    • 0033040441 scopus 로고    scopus 로고
    • Intracellular localization of oligonucleotides: Influence of fixative protocols
    • Pichon,C., Monsigny,M. and Roche,A.C. (1999) Intracellular localization of oligonucleotides: influence of fixative protocols. Antisense Nucleic Acid Drug Dev., 9, 89-93.
    • (1999) Antisense Nucleic Acid Drug Dev. , vol.9 , pp. 89-93
    • Pichon, C.1    Monsigny, M.2    Roche, A.C.3
  • 29
    • 0036289650 scopus 로고    scopus 로고
    • Positively charged DNA-binding proteins cause apparent cell membrane translocation
    • Lundberg,M. and Johansson,M. (2002) Positively charged DNA-binding proteins cause apparent cell membrane translocation. Biochem. Biophys. Res. Commun., 291, 367-371.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 367-371
    • Lundberg, M.1    Johansson, M.2
  • 32
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • Derossi,D., Chassaing,G. and Prochiantz,A. (1998) Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol., 8, 84-87.
    • (1998) Trends Cell Biol. , vol.8 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 33
    • 0013094825 scopus 로고    scopus 로고
    • Structure prediction of CPPs and iterative development of novel CPPs
    • Langel,U. (ed.), CRC Press LLC, Boca Raton, FL, USA
    • Bouffioux,O., Basyn,F., Rezsohazy,R. and Brasseur,R. (2002) Structure prediction of CPPs and iterative development of novel CPPs. In Langel,U. (ed.), Cell Penetrating Peptides. CRC Press LLC, Boca Raton, FL, USA, pp. 187-222.
    • (2002) Cell Penetrating Peptides , pp. 187-222
    • Bouffioux, O.1    Basyn, F.2    Rezsohazy, R.3    Brasseur, R.4


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