Messenger proteins: Homeoproteins, TAT and others

Current Opinion in Cell Biology

Volumn 12, Issue 4, 2000, Pages 400-406

  Prochiantz, Alain ^a  

^a CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

HOMEODOMAIN PROTEIN; SIGNAL PEPTIDE; TRANSACTIVATOR PROTEIN;

BIOTECHNOLOGY; CELL NUCLEUS; CYTOPLASM; ENDOCYTOSIS; INTERNALIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECRETION; PROTEIN TRANSPORT; REVIEW; SIGNAL TRANSDUCTION;

EID: 0033948268     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00108-3     Document Type: Review

References (48)

1. Derossi D., Chassaing G., Prochiantz A. Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol. 8:1998;84-87.
2. Lindgren M., Hällbrink M., Prochiantz A., Langel U. Cell-penetrating peptides. Trends Pharmacol Sci. 21:2000;99-103.
3. Schwarze S.R., Dowdy S.F. In vivo protein transduction: intracellular delivery of biologically active protein, compounds and DNA. Trends Pharmacol Sci. 21:2000;45-48.
4. Schwarze S.R., Ho A., Vocero-Akbani A., Dowdy S.F. In vivo protein transduction: delivery of a biologically active protein into the mouse. Science. 285:1999;1569-1572. In this paper, it is shown that intraperitoneal injections of β-galactosidase reporter protein genetically linked to the transduction domain of TAT result in the intracellular accumulation of the enzyme. The most striking observation is that β-galactosidase activity is found in all tissues, including within the brain parenchyme, thus demonstrating that the fusion protein has been able to cross the blood-brain barrier.
5. Rousselle C., Clair P., Lefauconnier J-M., Kackzorek M., Scherrmann J-M., Temsamani J. New advances in the transport of doxorubicin through the blood brain barrier by a peptide vector mediated strategy. Mol Pharmacol. 57:2000;679-686. The manuscript describes the use of two distinct peptides, Penetratin and Protegrin to address the transport of doxorubicin into the brain. Although the activity of the anti-cancer agent doxorubicin was not tested, the authors report that, compared to free doxorubicin, linkage to either peptide leads to a 10-fold increase in intracerebrum concentration.
6. Berlose J.P., Convert O., Derossi D., Brunissen A., Chassaing G. Conformational and associative behaviours of the third helix of Antennapedia homeodomain in membrane-mimetic environments. Eur J Biochem. 242:1996;372-386.
7. Derossi D., Calvet S., Trembleau A., Brunissen A., Chassaing G., Prochiantz A. Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J Biol Chem. 271:1996;18 188-18 193.
8. Joliot A., Trembleau A., Raposo G., Calvet S., Volovitch M., Prochiantz A. Association of Engrailed homeoproteins with vesicles presenting caveolae-like properties. Development. 124:1997;1865-1875.
9. Joliot A., Maizel A., Rosenberg D., Trembleau A., Dupas S., Volovitch M., Prochiantz A. Identification of a signal sequence necessary for the unconventional secretion of Engrailed homeoprotein. Curr Biol. 8:1998;856-863.
10. Maizel A., Bensaude O., Prochiantz A., Joliot A.H. A short region of its homeodomain is necessary for Engrailed nuclear export and secretion. Development. 126:1999;3183-3190. On the basis of sequence comparisons, it was proposed that the sequence necessary for the unconventional secretion of the Engrailed homeoprotein is a nuclear export sequence, and this is demonstrated in this paper. This paper, in addition to demonstrating that homeoproteins can shuttle between the nucleus and the cytoplasm, links nuclear export to unconventional secretion.
11. Gehring W.J. Homeo boxes in the study of development. Science. 236:1987;1245-1252.
12. Krumlauf R. Hox genes in vertebrate development. Cell. 78:1994;191-201.
13. Gehring W.J., Qian Y.Q., Billeter M., Furukubo-Tokunaga K., Schier A.F., Resendez-Perez D., Affolter M., Otting G., Wüthrich K. Homeodomain-DNA recognition. Cell. 78:1994;211-223.
14. Joyner A.L. Engrailed, Wnt and Pax genes regulate midbrain-hindbrain development. Trends Genet. 12:1996;15-20.
15. Loomis C.A., Kimmel R.A., Tong C-X., Michaud J., Joyner A.L. Analysis of the genetic pathway leading to the formation of ectopic apical ectodermal ridges in mouse Engrailed-1 mutant limbs. Development. 125:1998;1137-1148.
16. Chatelin L., Volovitch M., Joliot A.H., Perez F., Prochiantz A. Transcription factor Hoxa-5 is taken up by cells in culture and conveyed to their nuclei. Mech Dev. 55:1996;111-117.
17. Lucas W.J., Bouché-Pillon S., Jackson D.P., Nguyen L., Baker L., Ding B., Hake S. Selective trafficking of KNOTTED1 homeodomain protein and its mRNA through plasmodesmata. Science. 270:1995;1980-1983.
18. Matsuoka K., Bednarek S.Y. Protein transport within the plant cell endomembrane system: an update. Curr Opin Plant Biol. 1:1998;463-469.
19. Lazarowitz S.G. Probing plant cell structure and function with viral movement proteins. Curr Opin Plant Biol. 2:1999;332-338.
20. Pickard B.G., Beachy R.N. Intercellular connections are developmentally controlled to help move molecules through the plant. Cell. 98:1999;5-8. A timely review on the structure and function of plasmodesmata and movement proteins. It describes how plasmodesmata are used by endogeneous molecules and also by viruses to circulate through the plant.
21. Helland D.E., Welles J.L., Caputo A., Haseltine W.A. Transcellular transactivation by the human immunodeficiency virus type 1 tat protein. J Virol. 65:1991;4547-4549.
22. Ensoli B., Buonaguro L., Barillari G., Fiorelli V., Gendelman R., Morgan R.A., Wingfield P., Gallo R.C. Release, uptake, and effects of extracellular human immunodeficiency virus type 1 Tat protein on cell growth and viral transactivation. J Virol. 67:1993;277-287.
23. Elliott G., O'Hare P. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell. 88:1997;223-233.
24. Pomeranz L.E., Blaho J.A. Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection. J Virol. 73:1999;6769-6781. VP22, a protein capable of intercellular sliding, accumulates in the nucleus at late stages of infection. This adds to the list of proteins with intercellular sliding properties found in the nucleus. In addition, Pomeranz and Blako demonstrate that VP22 nuclear accumulation correlates with its phosphorylation.
25. He J., Furmanski P. Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. Nature. 373:1995;721-724.
26. Jans D.A., Hassan G. Nuclear targeting by growth factors, cytokines, and their receptors: a role in signaling? BioEssays. 5:1998;400-411.
27. Rothberg K.G., Heuser J.E., Donzell W.C., Ying Y.S., Glenney J.R., Anderson R.G. Caveolin, a protein component of caveolae membrane coats. Cell. 68:1992;673-682.
28. Conrad P.A., Smart E.J., Ying Y-S., Anderson R.G.W., Bloom G.S. Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps. J Cell Biol. 131:1995;1421-1433.
29. Liu P., Li W-P., Machleidt T., Anderson R.G.W. Identification of caveolin-1 in lipoprotein particles secreted by exocrine cells. Nat Cell Biol. 1:1999;369-375. It is clearly demonstrated that caveolin-1 can be found in the lumen of secretory vesicles in the exocrine pancreas. Following stimulation by secretagogues, caveolin-1 is released into the extracellular space where it associates with two high-density lipoproteins markers: ApoA1 and ApoE. This, in addition to shedding light on the secretion of a protein without a signal sequence, suggests that caveolin plays a role in intracellular and extracellular lipid transport.
30. Joliot A., Pernelle C., Deagostini-Bazin H., Prochiantz A. Antennapedia homeobox peptide regulates neural morphogenesis. Proc Natl Acad Sci USA. 88:1991;1864-1868.
31. Le Roux I., Joliot A.H., Bloch-Gallego E., Prochiantz A., Volovitch M. Neurotrophic activity of the Antennapedia homeodomain depends on its specific DNA-binding properties. Proc Natl Acad Sci USA. 90:1993;9120-9124.
32. Derossi D., Joliot A.H., Chassaing G., Prochiantz A. The third helix of Antennapedia homeodomain translocates through biological membranes. J Biol Chem. 269:1994;10 444-10 450.
33. Vives E., Brodin P., Lebleu B. A truncated HIV-1 Tat protein basic domain translocates through the plasma membrane and accumulates in the cell nucleus. J Biol Chem. 272:1997;16 010-16 017.
34. Rösch P., Willbord D. Is EIAV Tat protein a homeodomain? Science. 272:1996;1672.
35. Nakielny S., Dreyfuss G. Nuclear export of proteins and RNAs. Curr Opin Cell Biol. 9:1997;420-429.
36. Laliberte R.E., Eggler J., Gabel C.A. ATP treatment of human monocytes promotes caspase-1 maturation and externalisation. J Biol Chem. 274:1999;36 944-36 951.
37. Tarantini F., La Vallee T., Jackson A., Gamble S., Mouta Carreira C., Garfinkel S., Burgess W.H., Maciag T. The extravesicular domain of synaptotagmin-1 is released with the latent fibroblast growth factor-1 homodimer in response to heat shock. J Biol Chem. 273:1998;22 209-22 216.
38. Rubartelli A., Cozzolino F., Talio M., Sitia R. A novel secretory pathway for interleukin-1β, a protein lacking a signal sequence. EMBO J. 9:1990;1503-1510.
39. Rubartelli A., Sitia R. Entry of exogenous polypeptides into the nucleus of living cells: facts and speculations. Trends Cell Biol. 5:1995;409-412.
40. Siders W.M., Mizel S.B. Interleukin-1 beta secretion. A possible multistep process that is regulated in a cell type-specific manner. J Biol Chem. 270:1995;16 258-16 254.
41. Ward B.M., Lazarowitz S.G. Nuclear export in plants: use of geminivirus movement proteins for a cell-based export assay. Plant Cell. 11:1999;1267-1276. BR1, a movement protein capable of traversing between plant cells through plasmodesmata, has a nuclear export sequence of the Rev family. It adds to the list of proteins externalized and re-internalized that gain access to the nucleus, and can escape from the nucleus thanks to a nuclear export sequence.
42. Gutman C.R., Strittmatter W.J., Weisgraber K.H., Matthew W.D. Apolipoprotein E binds to and potentiates the biological activity of ciliary neurotrophic factor. J Neurosci. 17:1997;6114-6121.
43. Hamon Y., Luciani M-F., Becq F., Verrier B., Rubartelli A., Chimini G. Interleukin-1β secretion is impaired by inhibitors of the ATP binding cassette transporter, ABC1. Blood. 90:1997;2911-2915.
44. Duboule D. No milk today (my Hox have gone away). Proc Natl Acad Sci USA. 96:1999;322-323.
45. Adler R. Ciliary neurotrophic factor as an injury factor. Curr Opin Neurobiol. 3:1993;785-789.
46. Keresztes M., Boonstra J. Import(ance) of growth factors in the nucleus. J Cell Biol. 145:1999;421-424.
47. Briata P., Di Blas E., Gulisano M., Mallamaci A., Iannone R., Boncinelli E., Corte G. EMX1 homeoprotein is expressed in cell nuclei of the developing cerebal cortex and in the axons of the olfactory sensory neurons. Mech Dev. 57:1996;169-180.
48. Rivera Pomar R., Niessing D., Schmidt O.U., Gehring W.J., Jackle H. RNA binding and translational suppression by bicoid. Nature. 379:1996;746-749.