ADAMs and protein disulfide isomerase: The key to regulated cell-surface protein ectodomain shedding?

Biochemical Journal

Volumn 428, Issue 3, 2010, Pages

  Bass, Rosemary ^a   Edwards, Dylan R ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

ADAM17; Disulphide bond pattern; Metalloproteinase; Protein disulfide isomerase (PDI); Redox regulation; Shedding

Indexed keywords

ADAM10 ENDOPEPTIDASE; CELL SURFACE PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; PROTEIN DISULFIDE ISOMERASE; REACTIVE OXYGEN METABOLITE; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; ADAM PROTEIN; MEMBRANE PROTEIN; TUMOR NECROSIS FACTOR ALPHA;

CHEMICAL BOND; CRYSTALLOGRAPHY; ENZYME ACTIVITY; HELA CELL; HUMAN; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; NOTE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; CHEMISTRY; METABOLISM; PROTEIN TERTIARY STRUCTURE;

ANIMALIA;

ADAM PROTEINS; MEMBRANE PROTEINS; PROTEIN DISULFIDE-ISOMERASES; PROTEIN STRUCTURE, TERTIARY; TUMOR NECROSIS FACTOR-ALPHA;

EID: 77954896191     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100568     Document Type: Note

References (16)

1. Edwards, D. R., Handsley, M. M. and Pennington, C. J. (2008) The ADAM metalloproteinases. Mol. Aspects Med. 29, 258-289
2. Liu, H., Shim, A. H. and He, X. (2009) Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function. J. Biol. Chem. 284, 29077-29086
3. Murphy, G. (2008) The ADAMs: signalling scissors in the tumour microenvironment. Nat. Rev. Cancer 8, 929-941
4. Reddy, P., Slack, J. L., Davis, R., Cerretti, D. P., Kozlosky, C. J., Blanton, R. A., Shows, D., Peschon, J. J. and Black, R. A. (2000) Functional analysis of the domain structure of tumor necrosis factor-α converting enzyme. J. Biol. Chem. 275, 14608-14614
5. Janes, P. W., Wimmer-Kleikamp, S. H., Frangakis, A. S., Treble, K., Griesshaber, B., Sabet, O., Grabenbauer, M., Ting, A. Y., Saftig, P., Bastiaens, P. I. and Lackmann, M. (2009) Cytoplasmic relaxation of active Eph controls ephrin shedding by ADAM10. PLoS Biol. 7, e1000215
6. Maretzky, T., Le Gall, S. M., Worpenberg-Pietruk, S., Eder, J., Overall, C. M., Huang, X. Y., Poghosyan, Z., Edwards, D. R. and Blobel, C. P. (2009) Src stimulates fibroblast growth factor receptor-2 shedding by an ADAM15 splice variant linked to breast cancer. Cancer Res. 69, 4573-4576
7. Takeda, S., Igarashi, T., Mori, H. and Araki, S. (2006) Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold. EMBO J. 25, 2388-2396
8. Willems, S. H., Tape, C. J., Stanley, P. L., Taylor, N. A., Mills, I. G., Neal, D. E., McCafferty, J. and Murphy, G. (2010) Thiol isomerases negatively regulate the cellular shedding activity of ADAM17. Biochem. J. 429, 439-450
9. Appenzeller-Herzog, C. and Ellgaard, L. (2008) The human PDI family: versatility packed into a single fold. Biochim. Biophys. Acta 1783, 535-548
10. Boutet, P., Agüera-González, S., Atkinson, S., Pennington, C. J., Edwards, D. R., Murphy, G., Reyburn, H. T. and Valés-Gómez, M. (2009) Cutting edge: the metalloproteinase ADAM17/TNF-α-converting enzyme regulates proteolytic shedding of the MHC class I-related chain B protein. J. Immunol. 182, 49-53
11. Kaiser, B. K., Yim, D., Chow, I. T., Gonzalez, S., Dai, Z., Mann, H. H., Strong, R. K., Groh, V. and Spies, T. (2007) Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands. Nature 447, 482-486
12. Guan, H. H., Goh, K. S., Davamani, F., Wu, P. L., Huang, Y. W., Jeyakanthan, J., Wu, W. G. and Chen, C. J. (2010) Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins. J. Struct. Biol. 169, 294-303
13. Luo, B. H., Carman, C. V. and Springer, T. A. (2007) Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 25, 619-647
14. Lahav, J., Wijnen, E. M., Hess, O., Hamaia, S. W., Griffiths, D., Makris, M., Knight, C. G., Essex, D. W. and Farndale, R. W. (2003) Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin α2β1. Blood 102, 2085-2092
15. Swiatkowska, M., Szymański, J., Padula, G. and Cierniewski, C. S. (2008) Interaction and functional association of protein disulfide isomerase with αVβ3 integrin on endothelial cells. FEBS J. 275, 1813-1823.
16. Jordan, P. A. and Gibbins, J. M. (2006) Extracellular disulfide exchange and the regulation of cellular function. Antioxid. Redox Signaling 8, 312-323