HECT E3 Ubiquitin Ligase Nedd4-1 Ubiquitinates ACK and Regulates Epidermal Growth Factor (EGF)-Induced Degradation of EGF Receptor and ACK

REFERENCES

• Aoh, Q. L., A. M. Castle, C. H. Hubbard, O. Katsumata, and J. D. Castle. 2009. SCAMP3 negatively regulates EGFR degradation and promotes receptor recycling. Mol. Biol. Cell 20:1816–1832.
   PubMed Web of Science ®Google Scholar
• Authier, F., M. Métioui, A. W. Bell, and J. S. Mort. 1999. Negative regulation of epidermal growth factor signaling by selective proteolytic mechanisms in the endosome mediated by cathepsin B. J. Biol. Chem. 274:33723–33731.
   PubMedGoogle Scholar
• Bourdoulous, S., G. Orend, D. A. MacKenna, R. Pasqualini, and E. Ruoslahti. 1998. Fibronectin matrix regulates activation of RHO and CDC42 GTPases and cell cycle progression. J. Cell Biol. 143:267–276.
   PubMed Web of Science ®Google Scholar
• Chan, W., R. Tian, Y. F. Lee, S. T. Sit, L. Lim, and E. Manser. 2009. Down-regulation of active ACK1 is mediated by association with the E3 ubiquitin ligase Nedd4-2. J. Biol. Chem. 284:8185–8194.
   PubMed Web of Science ®Google Scholar
• Chen, H., C. A. Ross, N. Wang, Y. Huo, D. F. MacKinnon, J. B. Potash, S. G. Simpson, F. J. McMahon, J. R. DePaulo, Jr., and M. G. McInnis. 2001. NEDD4L on human chromosome 18q21 has multiple forms of transcripts and is a homologue of the mouse Nedd4-2 gene. Eur. J. Hum. Genet. 9:922–930.
   PubMed Web of Science ®Google Scholar
• Crawford, L. J., B. Walker, H. Ovaa, D. Chauhan, K. C. Anderson, T. C. Morris, and A. E. Irvine. 2006. Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132. Cancer Res. 66:6379–6386.
   PubMed Web of Science ®Google Scholar
• Eisenmann, K. M., J. B. McCarthy, M. A. Simpson, P. J. Keely, J. L. Guan, K. Tachibana, L. Lim, E. Manser, L. T. Furcht, and J. Iida. 1999. Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas. Nat. Cell Biol. 1:507–513.
   PubMed Web of Science ®Google Scholar
• Ekberg, J., F. Schuetz, N. A. Boase, S. J. Conroy, J. Manning, S. Kumar, P. Poronnik, and D. J. Adams. 2007. Regulation of the voltage-gated K(+) channels KCNQ2/3 and KCNQ3/5 by ubiquitination. Novel role for Nedd4-2. J. Biol. Chem. 282:12135–12142.
   PubMed Web of Science ®Google Scholar
• Elbashir, S. M., J. Harborth, W. Lendeckel, A. Yalcin, K. Weber, and T. Tuschl. 2001. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411:494–498.
   PubMed Web of Science ®Google Scholar
• Frey, M. R., R. S. Dise, K. L. Edelblum, and D. B. Polk. 2006. p38 kinase regulates epidermal growth factor receptor downregulation and cellular migration. EMBO J. 25:5683–5692.
   PubMedGoogle Scholar
• Galisteo, M. L., Y. Yang, J. Urena, and J. Schlessinger. 2006. Activation of the nonreceptor protein tyrosine kinase Ack by multiple extracellular stimuli. Proc. Natl. Acad. Sci. U. S. A. 103:9796–9801.
   PubMed Web of Science ®Google Scholar
• Goulet, C. C., K. A. Volk, C. M. Adams, L. S. Prince, J. B. Stokes, and P. M. Snyder. 1998. Inhibition of the epithelial Na+ channel by interaction of Nedd4 with a PY motif deleted in Liddle's syndrome. J. Biol. Chem. 273:30012–30017.
   PubMedGoogle Scholar
• Hackel, P. O., M. Gishizky, and A. Ullrich. 2001. Mig-6 is a negative regulator of the epidermal growth factor receptor signal. Biol. Chem. 382:1649–1662.
   PubMed Web of Science ®Google Scholar
• Hicke, L., and R. Dunn. 2003. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19:141–172.
   PubMed Web of Science ®Google Scholar
• Hopper, N. A., J. Lee, and P. W. Sternberg. 2000. ARK-1 inhibits EGFR signaling in C. elegans. Mol. Cell 6:65–75.
   PubMedGoogle Scholar
• Huang, F., D. Kirkpatrick, X. Jiang, S. Gygi, and A. Sorkin. 2006. Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol. Cell 21:737–748.
   PubMed Web of Science ®Google Scholar
• Ingham, R. J., G. Gish, and T. Pawson. 2004. The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture. Oncogene 23:1972–1984.
   PubMed Web of Science ®Google Scholar
• Katz, M., K. Shtiegman, P. Tal-Or, L. Yakir, Y. Mosesson, D. Harari, Y. Machluf, H. Asao, T. Jovin, K. Sugamura, and Y. Yarden. 2002. Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic 3:740–751.
   PubMedGoogle Scholar
• Leithe, E., and E. Rivedal. 2007. Ubiquitination of gap junction proteins. J. Membr. Biol. 217:43–51.
   PubMedGoogle Scholar
• Levkowitz, G., H. Waterman, E. Zamir, Z. Kam, S. Oved, W. Y. Langdon, L. Beguinot, B. Geiger, and Y. Yarden. 1998. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12:3663–3674.
   PubMed Web of Science ®Google Scholar
• Levkowitz, G., H. Waterman, S. A. Ettenberg, M. Katz, A. Y. Tsygankov, I. Alroy, S. Lavi, K. Iwai, Y. Reiss, A. Ciechanover, S. Lipkowitz, and Y. Yarden. 1999. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol. Cell 4:1029–1040.
   PubMed Web of Science ®Google Scholar
• Lin, Q., C. G. Lo, R. A. Cerione, and W. Yang. 2002. The Cdc42-target ACK2 interacts with SH3PX1 (sorting nexin 9) to regulate EGFR degradation. J. Biol. Chem. 277:10134–10138.
   PubMedGoogle Scholar
• Linseman, D. A., K. A. Heidenreich, and S. K. Fisher. 2001. Stimulation of M3 muscarinic receptors induces phosphorylation of the Cdc42 effector activated Cdc42Hs-associated kinase-1 via a Fyn tyrosine kinase signaling pathway. J. Biol. Chem. 276:5622–5628.
   PubMed Web of Science ®Google Scholar
• Longva, K. E., F. D. Blystad, E. Stang, A. M. Larsen, L. E. Johannessen, and I. H. Madshus. 2002. Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies. J. Cell Biol. 156:843–854.
   PubMed Web of Science ®Google Scholar
• Magnifico, A., S. Ettenberg, C. Yang, J. Mariano, S. Tiwari, S. Fang, S. Lipkowitz, and A. M. Weissman. 2003. WW domain HECT E3s target Cbl RING finger E3s for proteasomal degradation. J. Biol. Chem. 278:43169–43177.
   PubMedGoogle Scholar
• Mahajan, N. P., Y. E. Whang, J. L. Mohler, and H. S. Earp. 2005. Activated tyrosine kinase Ack1 promotes prostate tumorigenesis: role of Ack1 in polyubiquitination of tumor suppressor Wwox. Cancer Res. 65:10514–10523.
   PubMed Web of Science ®Google Scholar
• Mahajan, N. P., Y. Liu, S. Majumder, M. R. Warren, C. E. Parker, J. L. Mohler, H. S. Earp, and Y. E. Whang. 2007. Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 104:8438–8443.
   PubMed Web of Science ®Google Scholar
• Marmor, M. D., and Y. Yarden. 2004. Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases. Oncogene 23:2057–2070.
   PubMed Web of Science ®Google Scholar
• Rotin, D., O. Staub, and R. Haguenauer-Tsapis. 2000. Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J. Membr. Biol. 176:1–17.
   PubMed Web of Science ®Google Scholar
• Satoh, T., J. Kato, K. Nishida, and Y. Kaziro. 1996. Tyrosine phosphorylation of ACK in response to temperature shift-down, hyperosmotic shock, and epidermal growth factor stimulation. FEBS Lett. 386:230–234.
   PubMed Web of Science ®Google Scholar
• Sem, K. P., B. Zahedi, I. Tan, M. Deak, L. Lim, and N. Harden. 2002. ACK family tyrosine kinase activity is a component of Dcdc42 signaling during dorsal closure in Drosophila melanogaster. Mol. Cell. Biol. 22:3685–3697.
   PubMedGoogle Scholar
• Shen, F., Q. Lin, Y. Gu, C. Childress, and W. Yang. 2007. Activated Cdc42-associated kinase 1 (ACK1) is a component of EGF receptor signaling complex and regulates EGF receptor degradation. Mol. Biol. Cell 18:732–742.
   PubMed Web of Science ®Google Scholar
• Snyder, P. M., J. C. Steines, and D. R. Olson. 2004. Relative contribution of Nedd4 and Nedd4-2 to ENaC regulation in epithelia determined by RNA interference. J. Biol. Chem. 279:5042–5046.
   PubMedGoogle Scholar
• Sorkina, T., M. Miranda, K. R. Dionne, B. R. Hoover, N. R. Zahniser, and A. Sorkin. 2006. RNA interference screen reveals an essential role of Nedd4-2 in dopamine transporter ubiquitination and endocytosis. J. Neurosci. 26:8195–8205.
   PubMedGoogle Scholar
• Staub, O., S. Dho, P. Henry, J. Correa, T. Ishikawa, J. McGlade, and D. Rotin. 1996. WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome. EMBO J. 15:2371–2380.
   PubMed Web of Science ®Google Scholar
• Sudol, M., and T. Hunter. 2000. NeW wrinkles for an old domain. Cell 103:1001–1004.
   PubMed Web of Science ®Google Scholar
• Teo, M., L. Tan, L. Lim, and E. Manser. 2001. The tyrosine kinase ACK1 associates with clathrin-coated vesicles through a binding motif shared by arrestin and other adaptors. J. Biol. Chem. 276:18392–18398.
   PubMed Web of Science ®Google Scholar
• Thanos, C. D., K. E. Goodwill, and J. U. Bowie. 1999. Oligomeric structure of the human EphB2 receptor SAM domain. Science 283:833–836.
   PubMed Web of Science ®Google Scholar
• Tsubuki, S., Y. Saito, M. Tomioka, H. Ito, and S. Kawashima. 1996. Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine. J. Biochem. 119:572–576.
   PubMed Web of Science ®Google Scholar
• van Bemmelen, M. X., J. S. Rougier, B. Gavillet, F. Apotheloz, D. Daidie, M. Tateyama, I. Rivolta, M. A. Thomas, R. S. Kass, O. Staub, and H. Abriel. 2004. Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination. Circ. Res. 95:284–291.
   PubMed Web of Science ®Google Scholar
• van der Horst, E. H., Y. Y. Degenhardt, A. Strelow, A. Slavin, L. Chinn, J. Orf, M. Rong, S. Li, L. H. See, K. Q. Nguyen, T. Hoey, H. Wesche, and S. Powers. 2005. Metastatic properties and genomic amplification of the tyrosine kinase gene ACK1. Proc. Natl. Acad. Sci. U. S. A. 102:15901–15906.
   PubMed Web of Science ®Google Scholar
• Woelk, T., B. Oldrini, E. Maspero, S. Confalonieri, E. Cavallaro, P. P. Di Fiore, and S. Polo. 2006. Molecular mechanisms of coupled monoubiquitination. Nat. Cell Biol. 8:1246–1254.
   PubMedGoogle Scholar
• Xu, D., A. Makkinje, and J. M. Kyriakis. 2005. Gene 33 is an endogenous inhibitor of epidermal growth factor (EGF) receptor signaling and mediates dexamethasone-induced suppression of EGF function. J. Biol. Chem. 280:2924–2933.
   PubMedGoogle Scholar
• Yang, W., and R. A. Cerione. 1997. Cloning and characterization of a novel Cdc42-associated tyrosine kinase, ACK2, from bovine brain. J. Biol. Chem. 272:24819–24824.
   PubMed Web of Science ®Google Scholar
• Yang, W., C. G. Lo, T. Despenza, and R. A. Cerione. 2001. ACK2 directly interacts with clathrin and inhibits AP-2 mediated receptor endocytosis. J. Biol. Chem. 276:17468–17473.
   PubMedGoogle Scholar
• Yang, W., J. M. Jansen, Q. Lin, S. Canova, R. A. Cerione, and C. Childress. 2004. Interaction of activated Cdc42-associated tyrosine kinase ACK2 with HSP90. Biochem. J. 382:199–204.
   PubMed Web of Science ®Google Scholar
• Yang, W., Q. Lin, J. L. Guan, and R. A. Cerione. 1999. Activation of the Cdc42-associated tyrosine kinase-2 (ACK-2) by cell adhesion via integrin beta1. J. Biol. Chem. 274:8524–8530.
   PubMed Web of Science ®Google Scholar
• Zhang, X., K. A. Pickin, R. Bose, N. Jura, P. A. Cole, and J. Kuriyan. 2007. Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface. Nature 450:741–744.
   PubMed Web of Science ®Google Scholar
• Zhou, R., S. V. Patel, and P. M. Snyder. 2007. Nedd4-2 catalyzes ubiquitination and degradation of cell surface ENaC. J. Biol. Chem. 282:20207–20212.
   PubMed Web of Science ®Google Scholar