journal article Jan 01, 2005

ADAMs: key components in EGFR signalling and development

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References
144
[1]
Massague, J. & Pandiella, A. Membrane-anchored growth factors. Annu. Rev. Biochem. 62, 515–541 (1993). 10.1146/annurev.bi.62.070193.002503
[2]
Hooper, N. M., Karran, E. H. & Turner, A. J. Membrane protein secretases. Biochem. J. 321, 265–279 (1997). 10.1042/bj3210265
[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). 10.1042/bst0280441
[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). 10.1242/jcs.112.21.3603
[5]
ADAMs: focus on the protease domain

Roy A Black, Judith M White

Current Opinion in Cell Biology 1998 10.1016/s0955-0674(98)80042-2
[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). 10.1016/s0070-2153(03)54006-6
[7]
The ADAMs family of metalloproteases: multidomain proteins with multiple functions

Darren F. Seals, Sara A. Courtneidge

Genes & Development 2003 10.1101/gad.1039703
[8]
Kheradmand, F. & Werb, Z. Shedding light on sheddases: role in growth and development. Bioessays 24, 8–12 (2002). 10.1002/bies.10037
[9]
Moss, M. L. & Bartsch, J. W. Therapeutic benefits from targeting of ADAM family members. Biochemistry 43, 7227–7235 (2004). 10.1021/bi049677f
[10]
Untangling the ErbB signalling network

Yosef Yarden, Mark X. Sliwkowski

Nature Reviews Molecular Cell Biology 2001 10.1038/35052073
[11]
The discovery of receptor tyrosine kinases: targets for cancer therapy

Andreas Gschwind, Oliver M. Fischer, Axel Ullrich

Nature Reviews Cancer 2004 10.1038/nrc1360
[12]
Schlessinger, J. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 110, 669–672 (2002). 10.1016/s0092-8674(02)00966-2
[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). 10.1016/s1097-2765(03)00350-2
[14]
White, J. M. ADAMs: modulators of cell–cell and cell–matrix interactions. Curr. Opin. Cell Biol. 15, 598–606 (2003). 10.1016/j.ceb.2003.08.001
[15]
Mumm, J. S. & Kopan, R. Notch signaling: from the outside in. Dev. Biol. 228, 151–165 (2000). 10.1006/dbio.2000.9960
[16]
McFarlane, S. Metalloproteases: carving out a role in axon guidance. Neuron 37, 559–562 (2003). 10.1016/s0896-6273(03)00089-8
[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). 10.1385/jmn:17:2:171
[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). 10.1006/dbio.1995.1152
[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). 10.1083/jcb.111.1.69
[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). 10.1038/356248a0
[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). 10.1073/pnas.90.22.10783
[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). 10.1128/ec.3.1.27-39.2004
[23]
Wen, C., Metzstein, M. M. & Greenwald, I. SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signaling. Development 124, 4759–4767 (1997). 10.1242/dev.124.23.4759
[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). 10.1016/s0092-8674(00)80335-9
[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). 10.1042/bj3170045
[26]
Black, R. et al. A metalloprotease disintegrin that releases tumour-necrosis factor-α from cells. Nature 385, 729–733 (1997). 10.1038/385729a0
[27]
Moss, M. L. et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α. Nature 385, 733–736 (1997). 10.1038/385733a0
[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). 10.1074/jbc.273.27.16993
[29]
Roghani, M. et al. Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity. J. Biol. Chem. 274, 3531–3540 (1999). 10.1074/jbc.274.6.3531
[30]
Howard, L., Zheng, Y., Horrocks, M., Maciewicz, R. A. & Blobel, C. P. Catalytic activity of ADAM28. FEBS Lett. 498, 82–86 (2001). 10.1016/s0014-5793(01)02506-6
[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). 10.1006/bbrc.2000.4200
[32]
Schlomann, U. et al. The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion. J. Biol. Chem. 277, 48210–48219 (2002). 10.1074/jbc.m203355200
[33]
Chesneau, V. et al. Catalytic properties of ADAM19. J. Biol. Chem. 278, 22331–22340 (2003). 10.1074/jbc.m302781200
[34]
Zou, J. et al. Catalytic activity of human ADAM33. J. Biol. Chem. 279, 9818–9830 (2004). 10.1074/jbc.m309696200
[35]
Murphy, G. et al. Role of TIMPs (tissue inhibitors of metalloproteinases) in pericellular proteolysis: the specificity is in the detail. Biochem. Soc. Symp. 65–80 (2003). 10.1042/bss0700065
[36]
Loechel, F., Overgaard, M. T., Oxvig, C., Albrechtsen, 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). 10.1074/jbc.274.19.13427
[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). 10.1074/jbc.274.43.30563
[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). 10.1042/bj3480021
[39]
Gonzales, P. E. et al. Inhibition of the TNFα converting enzyme (TACE) by its pro domain. J. Biol. Chem. 279, 31638–31645 (2004). 10.1074/jbc.m401311200
[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). 10.1016/0955-0674(92)90098-w
[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). 10.1074/jbc.271.9.4593
[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). 10.1096/fasebj.11.2.9039960
[44]
Smith, K. M. et al. The cysteine-rich domain regulates ADAM protease function in vivo. J. Cell Biol. 159, 893–902 (2002). 10.1083/jcb.200206023
[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). 10.1074/jbc.275.19.14608
[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). 10.1083/jcb.132.4.717
[47]
Cho, C. et al. Fertilization defects in sperm from mice lacking fertilin β. Science 281, 1857–1859 (1998). 10.1126/science.281.5384.1857
[48]
Cho, C., Ge, H., Branciforte, D., Primakoff, P. & Myles, D. G. Analysis of mouse fertilin in wild-type and fertilin β (−/−) 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). 10.1006/dbio.2000.9703
[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). 10.1006/dbio.2001.0166
[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). 10.1016/s0378-1119(99)00208-5

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Published
Jan 01, 2005
Vol/Issue
6(1)
Pages
32-43
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Cite This Article
Carl P. Blobel (2005). ADAMs: key components in EGFR signalling and development. Nature Reviews Molecular Cell Biology, 6(1), 32-43. https://doi.org/10.1038/nrm1548
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