ADAMs: Key components in egfr signalling and development

Nature Reviews Molecular Cell Biology

Volumn 6, Issue 1, 2005, Pages 32-43

  Blobel, Carl P ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADAM PROTEIN; AMPHIREGULIN; AMYLOID PRECURSOR PROTEIN; BETACELLULIN; DIPEPTIDYL CARBOXYPEPTIDASE; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 4; EPIREGULIN; FERTILIN; FRACTALKINE; HEPARIN BINDING EPIDERMAL GROWTH FACTOR; L SELECTIN; METALLOPROTEINASE; PERVANADATE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN ADAM10; PROTEIN ADAM12; PROTEIN ADAM15; PROTEIN ADAM19; PROTEIN ADAM28; PROTEIN ADAM33; PROTEIN ADAM8; PROTEIN ADAM9; TRANSFORMING GROWTH FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR 2; UNCLASSIFIED DRUG; UNINDEXED DRUG;

ANGIOGENESIS; CANCER; DIMERIZATION; ENZYME ACTIVITY; ENZYME REGULATION; FERTILIZATION; HEART DEVELOPMENT; HUMAN; NERVOUS SYSTEM DEVELOPMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RECEPTOR BINDING; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; DIMERIZATION; HEART; HUMANS; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; NEOVASCULARIZATION, PHYSIOLOGIC; RECEPTOR, EPIDERMAL GROWTH FACTOR; SIGNAL TRANSDUCTION;

EID: 11244261160     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1548     Document Type: Review

References (144)

1. Massague, J. & Pandiella, A. Membrane-anchored growth factors. Annu. Rev. Biochem. 62, 515-541 (1993).
2. Hooper, N. M., Karran, E. H. & Turner, A. J. Membrane protein secretases. Biochem. J. 321, 265-279 (1997).
3. Hooper, N. M. & Turner, A. J. Protein processing mechanisms: from angiotensin-converting enzyme to Alzheimer's disease. Biochem. Soc. Trans. 28, 441-446 (2000).
4. Schlöndorff, J. & Blobel, C. P. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein ectodomain shedding. J. Cell Sci. 112, 3603-3617 (1999).
5. Black, R. A. & White, J. M. ADAMs: focus on the protease domain. Curr. Opin. Cell. Biol. 10, 654-659 (1998).
6. Becherer, J. D. & Blobel, C. P. Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs). Curr. Top. Dev. Biol. 54, 101-123 (2003).
7. Seals, D. F. & Courtneidge, S. A. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 17, 7-30 (2003).
8. Kheradmand, F. & Werb, Z. Shedding light on sheddases: role in growth and development. Bioessays 24, 8-12 (2002).
9. Moss, M. L. & Bartsch, J. W. Therapeutic benefits from targeting of ADAM family members. Biochemistry 43, 7227-7235 (2004).
10. Yarden, Y. & Sliwkowski, M. X. Untangling the ErbB signalling network. Nature Rev. Mol. Cell Biol. 2, 127-137 (2001).
11. Gschwind, A., Fischer, O. M. & Ullrich, A. The discovery of receptor tyrosine kinases: targets for cancer therapy. Nature Rev. Cancer 4, 361-370 (2004).
12. Schlessinger, J. Ligand-induced, receptor-mediated dimerization and actuation of EGF receptor. Cell 110, 669-672 (2002).
13. Burgess, A. W. et al. An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol. Cell 12, 541-552 (2003).
14. White, J. M. ADAMs: modulators of cell-cell and cell-matrix interactions. Curr. Opin. Cell Biol. 15, 598-606 (2003).
15. Mumm, J. S. & Kopan, R. Notch signaling: from the outside in. Dev. Biol. 228, 151-165 (2000).
16. McFarlane, S. Metalloproteases: carving out a role in axon guidance. Neuron 37, 559-562 (2003).
17. Hartmann, D., Tournoy, J., Saftig, P., Annaert, W. & de Strooper, B. Implication of APP secretases in notch signaling. J. Mol. Neurosci. 17, 171-181 (2001).
18. Wolfsberg, T. G. et al. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin domain and a metalloprotease domain. Dev. Biol. 169, 378-383 (1995).
19. Blobel, C. P., Myles, D. G., Primakoff, P. & White, J. W. Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence. J. Cell Biol. 111, 69-78 (1990).
20. Blobel, C. P. et al. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356, 248-252 (1992).
21. Wolfsberg, T. G. et al. The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional and evolutionary implications. Proc. Natl Acad. Sci. USA 90, 10783-10787 (1993).
22. Nakamura, T., Abe, H., Hirata, A. & Shimoda, C. ADAM family protein Mde10 is essential for development of spore envelopes in the fission yeast Schizosaccharomyces pombe. Eukaryot Cell 3, 27-39 (2004).
23. Wen, C., Metzstein, M. M. & Greenwald, I. SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophia KUZBANIAN, and its role in LIN-12/NOTCH signaling. Development 124, 4759-4767 (1997).
24. Pan, D. & Rubin, J. KUZBANIAN controls proteolytic processing of NOTCH and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 90, 271-280 (1997).
25. Howard, L., Lu, X., Mitchell, S., Griffiths, S. & Glynn, P. Molecular cloning of MADM: a catalytically active disintegrin-metalloprotease expressed in various cell types. Biochem. J. 317, 45-50 (1996).
26. Black, R. et al. A metalloprotease disintegrin that releases tumour-necrosis factor-α from cells. Nature 385, 729-733 (1997).
27. Moss, M. L. et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α. Nature 385, 733-736 (1997).
28. Loechel, F., Gilpin, B. J., Engvall, E., Albrechtsen, R. & Wewer, U. M. Human ADAM 12 (meltrin-α) is an active metalloprotease. J. Biol. Chem. 273, 16993-16997 (1998).
29. Roghani, M. et al. Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. J. Biol. Chem. 274, 3531-3540 (1999).
30. Howard, L., Zheng, Y., Horrocks, M., Maciewicz, R. A. & Blobel, C. P. Catalytic activity of ADAM28. FEBS Lett. 498, 82-86 (2001).
31. Wei, P., Zhao, Y. G., Zhuang, L., Ruben, S. & Sang, Q. X. Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin-β, Biochem. Biophys. Res. Commun. 280, 744-755 (2001).
32. Schlomann, U. et al. The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion. J. Biol. Chem. 277, 48210-18219 (2002).
33. Chesneau, V. et al. Catalytic properties of ADAM 19. J. Biol. Cnem. 278, 22331-22340 (2003).
34. Zou, J. et al. Catalytic activity of human ADAM33. J. Biol. Chem. 279, 9818-9830 (2004).
35. Murphy, G. et al. Role of TIMPs (tissue inhibtors of metalloproteinases) in pericellular proteolysis: the specificity is in the detail. Biochem. Soc. Symp. 65-80 (2003).
36. Loechel, F., Overgaard, M. T., Oxvig, C., Albrechlsen, R. & Wewer, U. M. Regulation of human ADAM 12 protease by the prodomain. Evidence for a functional cysteine switch. J. Biol. Chem. 274, 13427-13433 (1999).
37. Milla, M. E. et al. Specific sequence elements are required for the expression of functional tumor necrosis factor-α-converting enzyme (TACE). J. Biol. Chem. 274, 30563-30570 (1999).
38. Howard, L., Maciewicz, R. A. & Blobel, C. P. Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28. Biochem. J. 348, 21-27 (2000).
39. Gonzales, P. E. et al. Inhibition of the TNFα converting enzyme (TACE) by its pro domain. J. Biol. Chem. 279, 31638-31645 (2004).
40. Niewiarowski, S., McLane, M. A., Kloczewiak, M. & Stewart, G. J. Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors. Semin. Hematol. 31, 289-300 (1994).
41. Blobel, C. P. & White, J. M. Structure, function and evolutionary relationship of proteins containing a disintegrin domain. Curr. Opin. Cell Biol. 4, 760-765 (1992).
42. Krätzschmar, J., Lum, L. & Blobel, C. P. Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence. J. Biol. Chem. 271, 4593-4596 (1996).
43. Herren, B., Raines, E. W. & Ross, R. Expression of a disintegrin-like protein in cultured human vascular cells in vivo. FASEB J. 11, 173-180 (1997).
44. Smith, K. M. et al. The cysteine-rich domain regulates ADAM protease function in vivo. J. Cell Biol. 159, 893-902 (2002).
45. Reddy, P. et al. Functional analysis of the domain structure of tumor necrosis factor-α converting enzyme. J. Biol. Chem. 275, 14608-14614 (2000).
46. Weskamp, G., Krätzschmar, J. R., Reid, M. & Blobel, C. P. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J. Cell Biol. 132, 717-726 (1996).
47. Cho, C. et al. Fertilization defects in sperm from mice lacking fertilin β. Science 281, 1857-1859 (1998).
48. -/-) sperm: evidence for C-terminal modification, α/β dimerization, and lack of essential role of fertilin α in sperm-egg fusion. Dev. Biol. 222, 289-295. (2000).
49. Nishimura, H., Cho, C., Branciforte, D. R., Myles, D. G. & Primakoff, P. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β. Dev. Biol. 233, 204-213 (2001).
50. Zhu, G. Z., Lin, Y., Myles, D. G. & Primakoff, P. Identification of four novel ADAMs with potential roles in spermatogenesis and fertilization. Gene 234, 227-237 (1999).
51. Shamsadin, R. et al. Male mice deficient for germ-cell cyritestin are infertile. Biol. Reprod. 61, 1445-1451 (1999).
52. Leighton, P. A. et al. Defining brain wiring patterns and mechanisms through gene trapping in mice. Nature 410, 174-179 (2001).
53. Pandiella, A., Bosenberg, M., Huang, E. J., Besmer, P. & Massague, J. Cleavage of membrane-anchored growth factors involves distinct protease activities regulated through common mechanisms. J. Biol. Chem. 267, 24028-24033 (1992).
54. Arribas, J. & Massague, J. Transforming growth factor-α and β-amyloid precursor share a secretory mechanism. J. Cell Biol. 128, 433-441 (1995).
55. Anklesaria, P. et al. Cell-cell adhesion mediated by binding of membrane-anchored transforming growth factor α to epidermal growth factor receptors promotes cell proliferation. Proc. Natl Acad. Sci. USA 87, 3289-3293 (1990).
56. Wiley, H. S. et al. Removal of the membrane-anchoring domain of epidermal growth factor leads to intracrine signaling and disruption of mammary epithelial cell organization. J. Cell Biol. 143, 1317-1328 (1998).
57. Borrell-Pages, M., Rojo, F., Albanell, J., Baselga, J. & Arribas, J. TACE is required for the activation of the EGFR by TGF-α in tumors. EMBO J. 22, 1114-1124 (2003). Presents compelling evidence for an unexpected contribution of ectodomain shedding to juxtacrine signalling between TGFα and the EGFR.
58. McDermott, M. F. et al. Germline mutations in the extracellular domains of the 55 kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes. Cell 97, 133-144 (1999).
59. Hartmann, D. et al. The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for α-secretase activity in fibroblasts. Hum. Mol. Genet. 11, 2615-2624 (2002).
60. Lieber, T., Kidd, S. & Young, M. W. kuzbanian-mediated cleavage of Drosophila Notch. Genes Dev. 16, 209-221 (2002).
61. Brown, M. S., Ye, J., Rawson, R. B. & Goldstein, J. L. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100, 391-398 (2000).
62. Xia, W. & Wolfe, M. S. Intramembrane proteolysis by presenilin and presenilin-like proteases. J. Cell Sci. 116, 2839-2844 (2003).
63. Selkoe, D. & Kopan, R. Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu. Rev. Neurosci. 26, 565-597 (2003).
64. Bao, J., Wolpowitz, D., Role, L. W. & Talmage, D. A. Back signaling by the Nrg-1 intracellular domain. J. Cell Biol. 161, 1133-1141 (2003).
65. Nanba, D., Mammoto, A., Hashimoto, K. & Higashiyama, S. Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF. J. Cell Biol. 163, 489-502 (2003).
66. Harris, R. C., Chung, E. & Coffey, R. J. EGF receptor ligands. Exp. Cell Res. 284, 2-13 (2003).
67. Sahin, U. et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR-ligands. J. Cell Biol. 164, 769-779 (2004). Explores the contribution of different ADAMs to the shedding of six EGFR ligands using a loss-of-function approach with cells isolated from different ADAM-knockout mice.
68. Dong, J. et al., Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor. Proc. Natl Acad. Sci. USA 96, 6235-6240 (1999).
69. Fischer, O. M., Hart, S., Gschwind, A. & Ulrich, A. EGFR signal transactivation in cancer cells. Biochem. Soc. Trans. 31, 1203-1208 (2003).
70. Peschon, J. J. et al. An essential role for ectodomain shedding in mammalian development. Science 282, 1281-1284 (1998). Evaluation of mice lacking ADAM17 that uncovers a crucial role for ADAM17 in activating TGFα and the EGFR during mouse development.
71. Zhao, J. et al. Pulmonary hypoplasia in mice lacking tumor necrosis factor-α converting enzyme indicates an indispensable role for cell surface protein shedding during embryonic lung branching morphogenesis. Dev. Biol. 232, 204-218 (2001).
72. Jackson, L. F. et al. Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling. EMBO J. 22, 2704-2716 (2003). Elegant analysis of mice that lack HB-EGF or ADAM17 points towards a crucial role of ADAM17-dependent activation of HB-EGF during morphogenesis of heart valves in mice.
73. Iwamoto, R. et al. Heparin-binding EGF-like growth factor and ErbB signaling is essential for heart function. Proc. Natl Acad. Sci. USA 100, 3221-3226 (2003).
74. Shi, W. et al. TACE is required for fetal murine cardiac development and modeling. Dev. Biol. 261, 371-380 (2003).
75. Luetteke, N. C. et al. Targeted inactivation of the EGF and amphiregulin genes reveals distinct roles for EGF receptor ligands in mouse mammary gland development. Development 126, 2739-2750 (1999).
76. Merlos-Suarez, A., Ruiz-Paz, S., Baselga, J. & Arribas, J. Metalloprotease-dependent protransforming growth factor-α ectodomain shedding in the absence of tumor necrosis factor-α-converting enzyme. J. Biol. Chem. 276, 48510-48517 (2001).
77. Sunnarborg, S. W. et al. Tumor necrosis factor-α converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability. J. Biol. Chem. 277, 12838-12845 (2002).
78. Yamazaki, S. et al. Mice with defects in HB-EGF ectodomain shedding show severe developmental abnormalities. J. Cell Biol. 163, 469-475 (2003). Mice with a knock-in mutation that renders HB-EGF uncleavable have defects in heart-valve development that resemble those in mice that completely lack HB-EGF or ADAM17. This further corroborates the essential role of ectodomain shedding in the functional activation of HB-EGF.
79. Brachmann, R. et al. Transmembrane TGF-α precursors activate EGF/TGF-α receptors. Cell 56, 691-700 (1989).
80. Wong, S. T. et al. The TGF-α precursor expressed on the cell surface binds to the EGF receptor on adjacent cells, leading to signal transduction. Cell 56, 495-506 (1989).
81. Blasband, A. J. et al. Expression of the TGFα integral membrane precursor induces transformation of NRK cells. Oncogene 5, 1213-1221 (1990).
82. Yang, H. et al. Defective cleavage of membrane bound TGFα leads to enhanced activation of the EGF receptor in malignant cells. Oncogene 19, 1901-1914 (2000).
83. Higashiyama, S. et al. The membrane protein CD9/DRAP 27 potentiates the juxtacrine growth factor activity of the membrane-anchored heparin-binding EGF-like growth factor. J. Cell Biol. 128, 929-938 (1995).
84. Shi, W., Fan, H., Shum, L. & Derynck, R. The tetraspanin CD9 associates with transmembrane TGF-α and regulates TGF-α-induced EGF receptor activation and cell proliferation. J. Cell Biol. 148, 591-602 (2000).
85. Garrett, T. P. et al. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor α. Cell 110, 763-773 (2002).
86. Ogiso, H. et al. Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell 110, 775-787 (2002).
87. Jorissen, R. N. et al. Epidermal growth factor receptor: mechanisms of activation and signalling. Exp. Cell Res. 284, 31-53 (2003).
88. Mendelsohn, J. & Baselga, J. Status of epidermal growth factor receptor antagonists in the biology and treatment of cancer. J. Clin. Oncol. 21, 2787-2799 (2003).
89. Izumi, Y. et al. A metalloprotease-disintegrin, MDC9/meltrin-γ/ ADAMg and PKCδ are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J. 17, 7260-7272 (1998).
90. Asakura, M. et al. Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nature Med. 8, 35-40 (2002).
91. Kurisaki, T. et al. Phenotypic analysis of Meltrin α (ADAM12)-deficient mice: involvement of Meltrin α in adipogenesis and myogenesis. Mol. Cell. Biol. 23, 55-61 (2003).
92. Lemjabbar, H. & Basbaum, C. Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells. Nature Med. 8, 41-46 (2002).
93. Yan, Y., Shirakabe, K. & Werb, Z. The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors. J. Cell Biol. 158, 221-226 (2002).
94. Lemjabbar, H. et al. Tobacco smoke-induced lung cell proliferation mediated by tumor necrosis factor α-converting enzyme and amphiregulin. J. Biol. Chem. 278, 26202-26207 (2003).
95. Schafer, B., Gschwind, A. & Ulrich, A. Multiple G-protein-coupled receptor signals converge on the epidermal growth factor receptor to promote migration and invasion. Oncogene 23, 991-999 (2004).
96. Gschwind, A., Hart, S., Fischer, O. M. & Ulrich, A. TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells. EMBO J. 22, 2411-2421 (2003).
97. Cho, H. S. et al. Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature 421, 756-760 (2003).
98. Citri, A., Skaria, K. B. & Yarden, Y. The deaf and the dumb: the biology of ErbB-2 and ErbB-3. Exp. Cell Res. 284, 54-65 (2003).
99. Falls, D. L. Neuregulins: functions, forms, and signaling strategies. Exp. Cell Res. 284, 14-30 (2003).
100. Shirakabe, K., Wakatsuki, S., Kurisaki, T. & Fujisaswa-Sehara, A. Roles of Meltrin β/ADAM19 in the processing of neuregulin. J. Biol. Chem. 276, 9352-9358 (2001).
101. Kurohara, K. et al. Essential roles of Meltrin β (ADAM19) in heart development. Dev. Biol. 267, 14-28 (2004).
102. Zhou, H. M. et al. Essential role for ADAM19 in cardiovascular morphogenesis. Mol. Cell. Biol. 24, 96-104 (2004).
103. Diaz-Rodriguez, E., Esparis-Ogando, A., Montero, J. C., Yuste, L. & Pandiella, A. Stimulation of cleavage of membrane proteins by calmodulin inhibtors. Biochem. J. 346, 359-367 (2000).
104. Montero, J. C., Yuste, L., Diaz-Rodriguez, E., Esparis-Ogando, A. & Pandiella, A. Differential shedding of transmembrane neuregulin isoforms by the tumor necrosis factor-α-converting enzyme. Mol. Cell. Neurosci. 16, 631-648 (2000).
105. Molina, M. A. et al. Trastuzumab(herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells. Cancer Res. 61, 4744-4749 (2001).
106. Vecchi, M., Baulida, J. & Carpenter, G. Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C actuation. J. Biol. Chem. 271, 18989-18996 (1996).
107. Vecchi, M., Rudolph-Owen, L. A., Brown, C. L., Dempsey, P. J. & Carpenter, G. Tyrosine phosphorylation and proteolysis. Pervanadate-induced, metalloprotease-dependent cleavage of the ErbB-4 receptor and amphiregulin. J. Biol. Chem. 273, 20589-20595 (1998).
108. Ni, C. Y., Murphy, M. P., Golde, T. E. & Carpenter, G. γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 294, 2179-2181 (2001).
109. Carpenter, G. Nuclear localization and possible functions of receptor tyrosine kinases. Curr. Opin. Cell Biol. 15, 143-148 (2003).
110. Urban, S., Lee, J. R. & Freeman, M. A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands. EMBO J. 21, 4277-4286 (2002).
111. Urban, S., Lee, J. R. & Freeman, M. Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases. Cell 107, 173-182 (2001).
112. Lee, J. R., Urban, S., Garvey, C. F. & Freeman, M. Regulated intracellular ligand transport and proteolysis control EGF signal activation in Drosophila. Cell 107, 161-171 (2001).
113. Horiuchi, K. et al. Potential role for ADAM15 in pathological neovascularization in mice. Mol. Cell Biol. 23, 5614-5624 (2003).
114. Van Eerdewegh, P. et al. Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness. Nature 418, 426-430 (2002).
115. Arribas, J. et al. Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors. J. Biol. Chem. 271, 11376-11382 (1996).
116. Pandiella, A. & Massague, J. Cleavage of the membrane precursor for transforming growth factor α is a regulated process. Proc. Natl Acad. Sci. USA 88, 1726-1730 (1991).
117. Doedens, J. R., Mahimkar, R. M. & Black, R. A. TACE/ADAM-17 enzymatic activity is increased in response to cellular stimulation. Biochem. Biophys. Res. Commun. 308, 331-338 (2003).
118. Black, R. A. et al. Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity. Biochem. Soc. Symp. 70, 39-52 (2003).
119. Fan, H. & Derynck, R. Ectodomain shedding of TGF-α and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades. EMBO J. 18, 6962-6972 (1999).
120. Peiretti, F. et al. Identification of SAP97 as an intracellular binding partner of TACE. J. Cell Sci. 116, 1949-1957 (2003).
121. Nelson, K. K., Schlondorff, J. & Blobel, C. P. Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor α convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2β. Biochem. J. 343, 673-680 (1999).
122. Zheng, Y., Schlondorff, J. & Blobel, C. P. Evidence for regulation of the tumor necrosis factor α-convertase (TACE) by protein-tyrosine phosphatase PTPH1. J. Biol. Chem. 277, 42463-42470 (2002).
123. Cousin, H., Gaultier, A., Bleux, C., Darribere, T. & Alfandari, D. PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13. Dev. Biol. 227, 197-210 (2000).
124. Abram, C. L. et al. The adaptor protein Fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells. J. Biol. Chem. 278, 16844-16851 (2003).
125. Mori, S. et al. PACSIN3 binds ADAM12/meltrin α and up-regulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor. J. Biol. Chem. 278, 46029-46034 (2003).
126. Howard, L., Nelson, K. K., Maciewicz, R. A. & Blobel, C. P. Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. J. Biol. Chem. 274, 31693-31699 (1999).
127. Poghosyan, Z. et al. Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases. J. Biol. Chem. 277, 4999-5007 (2002).
128. Lammich, S. et al. Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc. Natl Acad Sci. USA 96, 3922-3927 (1999).
129. Kojro, E., Gimpl, G., Lammich, S., Marz, W. & Fahrenholz, F. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10. Proc. Natl Acad. Sci. USA 98, 5815-5820 (2001).
130. Matthews, V. et al. Cellular cholesterol depletion triggers shedding of the human interleukin-6 receptor by ADAM10 and ADAM17 (TACE). J. Biol. Chem. 278, 38829-38839 (2003).
131. Schlöndorff, J. S., Lum, L. & Blobel, C. P. Biochemical and pharmacological criteria define two shedding activities for TRANCE/OPGL that are distinct from the TNFα convertase (TACE). J. Biol. Chem. 276, 14665-14674 (2001).
132. Weskamp, G. et al. Evidence for a critical role of the TNFα convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR). J. Biol. Chem. 279, 4241-4249 (2004).
133. Zheng, Y., Saftig, P., Hartmann, D. & Blobel, C. Evaluation of the contribution of different ADAMs to TNFα shedding and of the function of the TNFα ectodomain in ensuring selective stimulated shedding by the TNFα convertase (TACE/ADAM17). J. Biol. Chem. 279, 42898-42906 (2004).
134. Alfalah, M. et al. A point mutation in the juxtamembrane stalk of human angiotensin I-converting enzyme invokes the action of a distinct secretase. J. Biol. Chem. 276, 21105-21109 (2001).
135. Petricoin, E. F. & Liotta, L. A. Proteomic analysis at the bedside: early detection of cancer. Trends Biotechnol. 20, S30-S34 (2002).
136. Liotta, L. A., Ferrari, M. & Petricoin, E. Clinical proteomics: written in blood. Nature 425, 905 (2003).
137. Tam, E. M., Morrison, C. J., Wu, Y. I., Stack, M. S. & Overall, C. M. Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl Acad. Sci. USA 101, 6917-6922 (2004).
138. Kelly, K. et al. Metalloprotease-disintegrin ADAM8: Expression analysis and targeted deletion in mice. Dev. Dyn. (in the press).
139. Weskamp, G. et al. Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life. Mol. Cell. Biol. 22, 1537-1544 (2002).
140. Prenzel, N. et al. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 402, 884-888 (1999). Crosstalk between GPCRs and the EGFR is shown to require the metalloprotease-dependent concept of a triple-membrane-passing signal.
141. Ferguson, K. M. et al. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol. Cell 11, 507-517 (2003).
142. Locksley, R. M., Killeen, N. & Lenardo, M. J. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104, 487-501 (2001).
143. Ruuls, S. R. et al. Membrane-bound TNF supports secondary lymphoid organ structure but is subservient to secreted TNF in driving autoimmune inflammation. Immunity 15, 533-543 (2001). Mice with a knock-in mutation that inactivates the cleavage site of TNFα are used to carefully dissect juxtacrine versus paracrine activities of this proinflammatory cytokine.
144. Blobel, C. P. Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNFα and Notch. Cell 90, 589-592 (1997).