Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold

EMBO Journal

Volumn 25, Issue 11, 2006, Pages 2388-2396

  Takeda, Soichi ^a,b   Igarashi, Tomoko ^a   Mori, Hidezo ^a   Araki, Satohiko ^c  

^a NATIONAL CEREBRAL AND CARDIOVASCULAR CENTER   (Japan)

^b RIKEN   (Japan)

^c NAGOYA UNIVERSITY   (Japan)

Author keywords

ADAM; MDC; Protein protein interaction shedding; Snake venom metalloproteinase

Indexed keywords

ADAM PROTEIN; CALCIUM ION; DISINTEGRIN; DISULFIDE; METALLOPROTEINASE; PROTEIN VAP1; SNAKE VENOM ANTISERUM; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; MAMMAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN STRUCTURE;

ADAM PROTEINS; AMINO ACID SEQUENCE; ANIMALS; APOPTOSIS REGULATORY PROTEINS; CROTALID VENOMS; CRYSTALLOGRAPHY, X-RAY; HUMANS; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

MAMMALIA;

EID: 33745731954     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601131     Document Type: Article

References (45)

1. Almeida EA, Huovila AP, Sutherland AE, Stephens LE, Calarco PG, Shaw LM, Mercurio AM, Sonnenberg A, Primakoff P, Myles DG, White JM (1995) Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor. Cell 81: 1095-1104
2. Becherer JD, Blobel CP (2003) Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs). Curr Top Dev Biol 54: 101-123
3. Black RA, Rauch CT, Kozlosky CJ, Peschon JJ, Slack JL, Wolfson MF, Castner BJ, Stocking KL, Reddy P, Srinivasan S, Nelson N, Boiani N, Schooley KA, Gerhart M, Davis R, Fitzner JN, Johnson RS, Paxton RJ, March CJ, Cerretti DP (1997) A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385: 729-733
4. Blobel CP (2005) ADAMs: key components in EGFR signalling and development. Nat Rev Mol Cell Biol 6: 32-43
5. Blobel CP, Myles DG, Primakoff P, White JM (1990) Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence. J Cell Biol 111: 69-78
6. Blobel CP, Wolfsberg TG, Turck CW, Myles DG, Primakoff P, White JM (1992) A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356: 248-252
7. Bode W, Gomis-Ruth FX, Stockler W (1993) Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett 331: 134-140
8. Bridges LC, Hanson KR, Tani PH, Mather T, Bowditch RD (2003) Integrin alpha4beta1-dependent adhesion to ADAM 28 (MDC-L) requires an extended surface of the disintegrin domain. Biochemistry 42: 3734-3741
9. Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D 54 (Part 5): 905-921
10. Calvete JJ, Marcinkiewicz C, Monleon D, Esteve V, Celda B, Juarez P, Sanz L (2005) Snake venom disintegrins: evolution of structure and function. Toxicon 45: 1063-1074
11. CCP4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
12. Duffy MJ, Lynn DJ, Lloyd AT, O'Shea CM (2003) The ADAMs family of proteins: from basic studies to potential clinical applications. Thromb Haemost 89: 622-631
13. Eto K, Huet C, Tarui T, Kupriyanov S, Liu HZ, Puzon-McLaughlin W, Zhang XP, Sheppard D, Engvall E, Takada Y (2002) Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions. J Biol Chem 277: 17804-17810
14. Evans JP (2001) Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. BioEssays 23: 628-639
15. Fox JW, Serrano SM (2005) Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 45: 969-985
16. Fujii Y, Okuda D, Fujimoto Z, Horii K, Morita T, Mizuno H (2003) Crystal structure of trimestatin, a disintegrin containing a cell adhesion recognition motif RGD. J Mol Biol 332: 1115-1122
17. Gaultier A, Cousin H, Darribere T, Alfandari D (2002) ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin. J Biol Chem 277: 23336-23344
18. Huang TF, Holt JC, Lukasiewicz H, Niewiarowski S (1987) Trigramin. A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein Iib-IIIa complex. J Biol Chem 262: 16157-16163
19. Iba K, Albrechtsen R, Gilpin B, Frohlich C, Loechel F, Zolkiewska A, Ishiguro K, Kojima T, Liu W, Langford JK, Sanderson RD, Brakebusch C, Fassler R, Wewer UM (2000) The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading. J Cell Biol 149: 1143-1156
20. Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E, Blobel CP, Himanen JP, Lackmann M, Nikolov DB (2005) Adam meets Eph: an ADAM substrate recognition module acts as a molecular SWITCH for Ephrin cleavage in trans. Cell 123: 291-304
21. Jia LG, Shimokawa K, Bjarnason JB, Fox JW (1996) Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins. Toxicon 34: 1269-1276
22. Jia LG, Wang XM, Shannon JD, Bjarnason JB, Fox JW (2000) Inhibition of platelet aggregation by the recombinant cysteine-rich domain of the hemorrhagic snake venom metalloproteinase, atrolysin A. Arch Biochem Biophys 373: 281-286
23. Kamiguti AS, Gallagher P, Marcinkiewicz C, Theakston RD, Zuzel M, Fox JW (2003) Identification of sites in the cysteine-rich domain of the class P-III snake venom metalloproteinases responsible for inhibition of platelet function. FEBS Lett 549: 129-134
24. Maskos K, Fernandez-Catalan C, Huber R, Bourenkov GP, Bartunik H, Ellestad GA, Reddy P, Wolfson MF, Rauch CT, Castner BJ, Davis R, Clarke HR, Petersen M, Fitzner JN, Cerretti DP, March CJ, Paxton RJ, Black RA, Bode W (1998) Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme. Proc Natl Acad Sci USA 95: 3408-3412
25. Masuda S, Hayashi H, Araki S (1998) Two vascular apoptosis-inducing proteins from snake venom are members of the metalloprotease/disintegrin family. Eur J Biochem 253: 36-41
26. Masuda S, Ohta T, Kaji K, Fox JW, Hayashi H, Araki S (2000) cDNA cloning and characterization of vascular apoptosis-inducing protein 1. Biochem Biophys Res Commun 278: 197-204
27. Moss ML, Bartsch JW (2004) Therapeutic benefits from targeting of ADAM family members. Biochemistry 43: 7227-7235
28. Moss ML, Jin SL, Milla ME, Bickett DM, Burkhart W, Carter HL, Chen WJ, Clay WC, Didsbury JR, Hassler D, Hoffman CR, Kost TA, Lambert MH, Leesnitzer MA, McCauley P, McGeehan G, Mitchell J, Moyer M, Pahel G, Rocque W, Overton LK, Schoenen F, Seaton T, Su JL, Warner J, Willard D, Becherer JD (1997) Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 385: 733-736
29. Myles DG, Kimmel LH, Blobel CP, White JM, Primakoff P (1994) Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion. Proc Natl Acad Sci USA 91: 4195-4198
30. Nakamura T, Abe H, Hirata A, Shimoda C (2004) ADAM family protein MdelO is essential for development of spore envelopes in the fission yeast Schizosaccharomyces pombe. Eukaryot Cell 3: 27-39
31. Orth P, Reichert P, Wang W, Prosise WW, Yarosh-Tomaine T, Hammond G, Ingram RN, Xiao L, Mirza UA, Zou J, Strickland C, Taremi SS, Le HV, Madison V (2004) Crystal structure of the catalytic domain of human ADAM33. J Mol Biol 335: 129-137
32. Pan D, Rubin GM (1997) Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 90: 271-280
33. Perrakis A, Morris R, Lamzin VS (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6: 458-463
34. Primakoff P, Hyatt H, Tredick-Kline J (1987) Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J Cell Biol 104: 141-149
35. Qi H, Rand MD, Wu X, Sestan N, Wang W, Rakic P, Xu T, Artavanis-Tsakonas S (1999) Processing of the notch ligand delta by the metalloprotease Kuzbanian. Science 283: 91-94
36. Reddy P, Slack JL, Davis R, Cerretti DP, Kozlosky CJ, Blanton RA, Shows D, Peschon JJ, Black RA (2000) Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme. J Biol Chem 275: 14608-14614
37. Rooke J, Pan D, Xu T, Rubin GM (1996) KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis. Science 273: 1227-1231
38. Seals DF, Courtneidge SA (2003) The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 17: 7-30
39. Serrano SM, Jia LG, Wang D, Shannon JD, Fox JW (2005) Function of the cysteine-rich domain of the haemorrhagic metalloproteinase atrolysin A: targeting adhesion proteins collagen I and von Willebrand factor. Biochem J 391: 69-76
40. Smith KM, Gaultier A, Cousin H, Alfandari D, White JM, DeSimone DW (2002) The cysteine-rich domain regulates ADAM protease function in vivo. J Cell Biol 159: 893-902
41. Van Eerdewegh P, Little RD, Dupuis J, Del Mastro RG, Falls K, Simon J, Torrey D, Pandit S, McKenny J, Braunschweiger K, Walsh A, Liu Z, Hayward B, Folz C, Manning SP, Bawa A, Saracino L, Thackston M, Benchekroun Y, Capparell N, Wang M, Adair R, Feng Y, Dubois J, FitzGerald MG, Huang H, Gibson R, Allen KM, Pedan A, Danzig MR, Umland SP, Egan RW, Cuss FM, Rorke S, Clough JB, Holloway JW, Holgate ST, Keith TP (2002) Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness. Nature 418: 426-430
42. White JM (2003) ADAMs: modulators of cell-cell and cell-matrix interactions. Curr Opin Cell Biol 15: 598-606
43. Yagami-Hiromasa T, Sato T, Kurisaki T, Kamijo K, Nabeshima Y, Fujisawa-Sehara A (1995) A metalloprotease-disintegrin participating in myoblast fusion. Nature 377: 652-656
44. Zhu X, Teng M, Niu L (1999) Structure of acutolysin-C, a haemorrhagic toxin from the venom of Agkistrodon acutus, providing further evidence for the mechanism of the pH-dependent proteolytic reaction of zinc metalloproteinases. Acta Crystallogr D 55: 1834-1841
45. Zolkiewska A (1999) Disintegrin-like/cysteine-rich region of ADAM 12 is an active cell adhesion domain. Exp Cell Res 252: 423-431