Endocytosis and cancer

Current Opinion in Cell Biology

Volumn 16, Issue 2, 2004, Pages 156-161

  Polo, Simona ^a,b   Pece, Salvatore ^b,c   Di Fiore, Pier Paolo ^a,b,c  

^a FIRC INSTITUTE OF MOLECULAR ONCOLOGY   (Italy)

^b EUROPEAN INSTITUTE OF ONCOLOGY   (Italy)

^c UNIVERSITY OF MILAN   (Italy)

Author keywords

EGFR; epithelial growth factor receptor; Necd; Notch extracellular domain; receptor tyrosine kinase; RTK; sensory organ precursor; SOP

Indexed keywords

BETA CATENIN; CAVEOLIN 1; CLATHRIN; EPIDERMAL GROWTH FACTOR RECEPTOR; GUANOSINE TRIPHOSPHATASE; PROTEIN TYROSINE KINASE; TRANSFORMING GROWTH FACTOR BETA; UVOMORULIN;

BREAST CANCER; CANCER; CARCINOGENESIS; CELL PROLIFERATION; CELL SURFACE; DOWN REGULATION; ENDOCYTOSIS; ENZYME ACTIVATION; EUKARYOTIC CELL; GENE LOCUS; MORPHOGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; REVIEW; SIGNAL TRANSDUCTION; TUMOR GROWTH; UBIQUITINATION;

ANIMALS; CELL CYCLE PROTEINS; CELL DIVISION; CELL TRANSFORMATION, NEOPLASTIC; ENDOCYTOSIS; HUMANS; MEMBRANE PROTEINS; PROTEIN TRANSPORT; RECEPTOR PROTEIN-TYROSINE KINASES; SIGNAL TRANSDUCTION; UBIQUITIN;

EUKARYOTA;

EID: 2942615072     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.02.003     Document Type: Review

References (51)

1. Sorkin A., Von Zastrow M. Signal transduction and endocytosis: close encounters of many kinds. Nat Rev Mol Cell Biol. 3:2002;600-614
2. Conner S.D., Schmid S.L. Regulated portals of entry into the cell. Nature. 422:2003;37-44
3. Patapoutian A., Reichardt L.F. Trk receptors: mediators of neurotrophin action. Curr Opin Neurobiol. 11:2001;272-280
4. Gonzalez-Gaitan M. Signal dispersal and transduction through the endocytic pathway. Nat Rev Mol Cell Biol. 4:2003;213-224
5. Seto E.S., Bellen H.J., Lloyd T.E. When cell biology meets development: endocytic regulation of signaling pathways. Genes Dev. 16:2002;1314-1336
6. Parton R.G., Richards A.A. Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms. Traffic. 4:2003;724-738
7. Shen Q., Temple S. Creating asymmetric cell divisions by skewing endocytosis. Sci STKE. 2002:2002;PE52
8. Floyd S., De Camilli P. Endocytosis proteins and cancer: a potential link? Trends Cell Biol. 8:1998;299-301
9. Aguilar R.C., Wendland B. Ubiquitin: not just for proteasomes anymore. Curr Opin Cell Biol. 15:2003;184-190
10. Di Fiore P.P., Polo S., Hofmann K. When ubiquitin meets ubiquitin receptors: a signalling connection. Nat Rev Mol Cell Biol. 4:2003;491-497
11. Pickart C.M. Ubiquitin in chains. Trends Biochem Sci. 25:2000;544-548
12. Hicke L. Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol. 9:1999;107-112
13. Haglund K., Sigismund S., Polo S., Szymkiewicz I., Di Fiore P.P., Dikic I. Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat Cell Biol. 5:2003;461-466 This paper demonstrates that EGFR and PDGFR are monoubiquitinated at multiple sites and that replacement of the intracellular portion of EGFR with a single ubiquitin is sufficient to drive its internalisation and degradation.
14. Dikic I., Szymkiewicz I., Soubeyran P. Cbl signaling networks in the regulation of cell function. Cell Mol Life Sci. 60:2003;1805-1827
15. Bao J., Gur G., Yarden Y. Src promotes destruction of c-Cbl: implications for oncogenic synergy between Src and growth factor receptors. Proc Natl Acad Sci U S A. 100:2003;2438-2443 This study addresses the mechanism of Src-EGFR functional interaction: activation of Src leads to polyubiquitination and degradation of c-Cbl, which enables EGFR to escape internalisation.
16. Tice D.A., Biscardi J.S., Nickles A.L., Parsons S.J. Mechanism of biological synergy between cellular Src and epidermal growth factor receptor. Proc Natl Acad Sci U S A. 96:1999;1415-1420
17. Summy J.M., Gallick G.E. Src family kinases in tumor progression and metastasis. Cancer Metastasis Rev. 22:2003;337-358
18. Wu W.J., Tu S., Cerione R.A. Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation. Cell. 114:2003;715-725 This paper illustrates how Cdc42 can antagonise the Cbl-catalysed ubiquitination of EGF receptor. Activated Cdc42 forms a complex with β-Pix, which in turn associates with c-Cbl, preventing it from binding to EGFR.
19. Lozano E., Betson M., Braga V.M. Tumor progression: small GTPases and loss of cell-cell adhesion. Bioessays. 25:2003;452-463
20. Etienne-Manneville S., Hall A. Rho GTPases in cell biology. Nature. 420:2002;629-635
21. Christofori G. Split personalities: the agonistic antagonist Sprouty. Nat Cell Biol. 5:2003;377-379
22. Hanafusa H., Torii S., Yasunaga T., Nishida E. Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway. Nat Cell Biol. 4:2002;850-858 This paper shows that the inhibitory activity of Sprouty1 and 2 is triggered by their tyrosine phosphorylation. This leads to binding to Grb2 and displacement of the Grb2-Sos complex from the activated receptor.
23. Yusoff P., Lao D.H., Ong S.H., Wong E.S., Lim J., Lo T.L., Leong H.F., Fong C.W., Guy G.R. Sprouty2 inhibits the Ras/MAP kinase pathway by inhibiting the activation of Raf. J Biol Chem. 277:2002;3195-3201 This work supports the idea that Sprouty inhibits the Ras/MAP kinase pathway downstream of activated Ras, at the level of Raf.
24. Sasaki A., Taketomi T., Kato R., Saeki K., Nonami A., Sasaki M., Kuriyama M., Saito N., Shibuya M., Yoshimura A. Mammalian Sprouty4 suppresses Ras-independent ERK activation by binding to Raf1. Nat Cell Biol. 5:2003;427-432 This paper shows that RTKs use distinct pathways for Raf/ERK activation and that Sprouty4 suppresses VEGFR-induced, Ras-independent activation of Raf1 but does not affect EGFR-induced, Ras-dependent activation of Raf.
25. ••].
26. ••].
27. ••].
28. ••] together demonstrate that, upon EGF stimulation, Sprouty2 becomes tyrosine-phosphorylated and this enhances its interaction with Cbl. In turn, this prevents Cbl from downregulating EGFR. In addition, the Cbl-Sprouty2 interaction also leads to ubiquitination and degradation of the latter, thus providing a negative feedback control mechanism.
29. Yarden Y., Sliwkowski M.X. Untangling the ErbB signalling network. Nat Rev Mol Cell Biol. 2:2001;127-137
30. Pelkmans L., Helenius A. Endocytosis via caveolae. Traffic. 3:2002;311-320
31. Nabi I.R., Le P.U. Caveolae/raft-dependent endocytosis. J Cell Biol. 161:2003;673-677
32. Di Guglielmo G.M., Le Roy C., Goodfellow A.F., Wrana J.L. Distinct endocytic pathways regulate TGF-β receptor signalling and turnover. Nat Cell Biol. 5:2003;410-421 This paper demonstrates that TGF-β receptors internalise through both caveolin- and clathrin-mediated pathways, but that these two routes produce different fates. Clathrin-dependent internalisation into EEA1-positive endosomes, where the Smad2 anchor SARA is enriched, promotes TGF-β signalling. Conversely, caveolar-dependent internalisation leads to Smad7-Smurf2-mediated ubiquitination promoting rapid receptor turnover.
33. Lipkowitz S. The role of the ubiquitination-proteasome pathway in breast cancer: ubiquitin mediated degradation of growth factor receptors in the pathogenesis and treatment of cancer. Breast Cancer Res. 5:2003;8-15
34. Hayashi K., Matsuda S., Machida K., Yamamoto T., Fukuda Y., Nimura Y., Hayakawa T., Hamaguchi M. Invasion activating caveolin-1 mutation in human scirrhous breast cancers. Cancer Res. 61:2001;2361-2364
35. Carver L.A., Schnitzer J.E. Caveolae: mining little caves for new cancer targets. Nat Rev Cancer. 3:2003;571-581
36. Yap A.S., Brieher W.M., Gumbiner B.M. Molecular and functional analysis of cadherin-based adherens junctions. Annu Rev Cell Dev Biol. 13:1997;119-146
37. Behrens J., Vakaet L., Friis R., Winterhager E., Van Roy F., Mareel M.M., Birchmeier W. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-SRC gene. J Cell Biol. 120:1993;757-766
38. Perl A.K., Wilgenbus P., Dahl U., Semb H., Christofori G. A causal role for E-cadherin in the transition from adenoma to carcinoma. Nature. 392:1998;190-193
39. Thiery J.P. Epithelial-mesenchymal transitions in tumour progression. Nat Rev Cancer. 2:2002;442-454
40. Weidner K.M., Behrens J., Vandekerckhove J., Birchmeier W. Scatter factor: molecular characteristics and effect on the invasiveness of epithelial cells. J Cell Biol. 111:1990;2097-2108
41. Fujita Y., Krause G., Scheffner M., Zechner D., Leddy H.E., Behrens J., Sommer T., Birchmeier W. Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex. Nat Cell Biol. 4:2002;222-231 The authors show that Hakai is a E3-ligase that, by interacting with E-cadherin in a phosphotyrosine-dependent fashion, induces its ubiquitination. Overexpression of Hakai disrupts cell-cell interaction and E-cadherin internalisation.
42. Artavanis-Tsakonas S., Rand M.D., Lake R.J. Notch signaling: cell fate control and signal integration in development. Science. 284:1999;770-776
43. Mumm J.S., Kopan R. Notch signaling: from the outside in. Dev Biol. 228:2000;151-165
44. Seugnet L., Simpson P., Haenlin M. Requirement for dynamin during Notch signaling in Drosophila neurogenesis. Dev Biol. 192:1997;585-598
45. Lai E.C., Deblandre G.A., Kintner C., Rubin G.M. Drosophila neuralized is a ubiquitin ligase that promotes the internalization and degradation of delta. Dev Cell. 1:2001;783-794
46. Itoh M., Kim C.H., Palardy G., Oda T., Jiang Y.J., Maust D., Yeo S.Y., Lorick K., Wright G.J., Ariza-McNaughton L., et al. Mind bomb is a ubiquitin ligase that is essential for efficient activation of Notch signaling by Delta. Dev Cell. 4:2003;67-82 This study shows that Mind bomb is an ubiquitin ligase and a positive regulator of Notch signalling in Zebrafish by promoting ubiquitination and endocytosis of the Delta ligand.
47. Guo M., Jan L.Y., Jan Y.N. Control of daughter cell fates during asymmetric division: interaction of Numb and Notch. Neuron. 17:1996;27-41
48. Santolini E., Puri C., Salcini A.E., Gagliani M.C., Pelicci P.G., Tacchetti C., Di Fiore P.P. Numb is an endocytic protein. J Cell Biol. 151:2000;1345-1352
49. Berdnik D., Torok T., Gonzalez-Gaitan M., Knoblich J.A. The endocytic protein α-Adaptin is required for numb-mediated asymmetric cell division in Drosophila. Dev Cell. 3:2002;221-231 In this study, it is shown that α-adaptin is asymmetrically localised at mitosis as a consequence of its interaction with Numb, suggesting that the asymmetric partitioning of the endocytic machinery acts downstream of asymmetrically distributed Numb in the polarised endocytosis of the Notch receptor.
50. Weijzen S., Rizzo P., Braid M., Vaishnav R., Jonkheer S.M., Zlobin A., Osborne B.A., Gottipati S., Aster J.C., Hahn W.C., et al. Activation of Notch-1 signaling maintains the neoplastic phenotype in human Ras-transformed cells. Nat Med. 8:2002;979-986
51. Al-Hajj M., Wicha M.S., Benito-Hernandez A., Morrison S.J., Clarke M.F. Prospective identification of tumorigenic breast cancer cells. Proc Natl Acad Sci U S A. 100:2003;3983-3988