Jagged-1 juxtamembrane region: Biochemical characterization and cleavage by ADAM17 (TACE) catalytic domain

Biochemical and Biophysical Research Communications

Volumn 432, Issue 4, 2013, Pages 666-671

  Coglievina, Maristella ^a   Guarnaccia, Corrado ^a   Zlatev, Ventsislav ^a   Pongor, Sándor ^a   Pintar, Alessandro ^a  

^a INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Italy)

Author keywords

Alagille syndrome; Circular dichroism; Ectodomain shedding; Mass spectrometry; Metalloprotease; Notch signaling

Indexed keywords

JAGGED1; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

ALAGILLE SYNDROME; ARTICLE; BIOCHEMISTRY; CATALYSIS; GENE MUTATION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ADAM PROTEINS; AMINO ACID SEQUENCE; CALCIUM-BINDING PROTEINS; CATALYTIC DOMAIN; HUMANS; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; LIGANDS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROTEOLYSIS; RECEPTORS, NOTCH;

EID: 84875543353     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.02.022     Document Type: Article

References (23)

1. LaVoie M.J., Selkoe D.J. The Notch ligands, Jagged and Delta, are sequentially processed by alpha-secretase and presenilin/gamma-secretase and release signaling fragments. J. Biol. Chem. 2003, 278:34427-34437.
2. Groot A.J., Vooijs M.A. The role of Adams in Notch signaling. Adv. Exp. Med. Biol. 2012, 727:15-36.
3. Jorissen E., De Strooper B. Gamma-secretase and the intramembrane proteolysis of Notch. Curr. Top. Dev. Biol. 2010, 92:201-230.
4. Parr-Sturgess C.A., Rushton D.J., Parkin E.T. Ectodomain shedding of the Notch ligand Jagged1 is mediated by ADAM17, but is not a lipid-raft-associated event. Biochem. J. 2010, 432:283-294.
5. van Goor H., Melenhorst W.B., Turner A.J., Holgate S.T. Adamalysins in biology and disease. J. Pathol. 2009, 219:277-286.
6. Manzetti S., McCulloch D.R., Herington A.C., van der Spoel D. Modeling of enzyme-substrate complexes for the metalloproteases MMP-3, ADAM-9 and ADAM-10. J. Comput. Aided Mol. Des. 2003, 17:551-565.
7. Caescu C.I., Jeschke G.R., Turk B.E. Active-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10. Biochem. J. 2009, 424:79-88.
8. Scheller J., Chalaris A., Garbers C., Rose-John S. ADAM17: a molecular switch to control inflammation and tissue regeneration. Trends Immunol. 2011, 32:380-387.
9. Mohan M.J., Seaton T., Mitchell J., Howe A., Blackburn K., Burkhart W., Moyer M., Patel I., Waitt G.M., Becherer J.D., Moss M.L., Milla M.E. The tumor necrosis factor-alpha converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity. Biochemistry 2002, 41:9462-9469.
10. Lambert M.H., Blackburn R.K., Seaton T.D., Kassel D.B., Kinder D.S., Leesnitzer M.A., Bickett D.M., Warner J.R., Andersen M.W., Badiang J.G., Cowan D.J., Gaul M.D., Petrov K.G., Rabinowitz M.H., Wiethe R.W., Becherer J.D., McDougald D.L., Musso D.L., Andrews R.C., Moss M.L. Substrate specificity and novel selective inhibitors of TNF-alpha converting enzyme (TACE) from two-dimensional substrate mapping. Comb. Chem. High Throughput Screen. 2005, 8:327-339.
11. Lai Z.W., Hanchapola I., Steer D.L., Smith A.I. Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site identification: determinants and constraints. Biochemistry 2011, 50:5182-5194.
12. Tang P., Hung M.C., Klostergaard J. Length of the linking domain of human pro-tumor necrosis factor determines the cleavage processing. Biochemistry 1996, 35:8226-8233.
13. Althoff K., Mullberg J., Aasland D., Voltz N., Kallen K., Grotzinger J., Rose-John S. Recognition sequences and structural elements contribute to shedding susceptibility of membrane proteins. Biochem. J. 2001, 353:663-672.
14. Warthen D.M., Moore E.C., Kamath B.M., Morrissette J.J., Sanchez P., Piccoli D.A., Krantz I.D., Spinner N.B. Jagged1 (JAG1) mutations in Alagille syndrome: increasing the mutation detection rate. Hum. Mutat. 2006, 27:436-443.
15. Piccoli D.A., Spinner N.B. Alagille syndrome and the Jagged1 gene. Semin. Liver Dis. 2001, 21:525-534.
16. Kelley L.A., Sternberg M.J. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 2009, 4:363-371.
17. Rawlings N.D., Barrett A.J., Bateman A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 2012, 40:D343-350.
18. Crooks G.E., Hon G., Chandonia J.M., Brenner S.E. WebLogo: a sequence logo generator. Genome Res. 2004, 14:1188-1190.
19. Whitmore L., Wallace B.A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 2008, 89:392-400.
20. Chen Y.H., Yang J.T., Chau K.H. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 1974, 13:3350-3359.
21. Dolnik O., Volchkova V., Garten W., Carbonnelle C., Becker S., Kahnt J., Stroher U., Klenk H.D., Volchkov V. Ectodomain shedding of the glycoprotein GP of Ebola virus. EMBO J. 2004, 23:2175-2184.
22. Nashine V.C., Hammes-Schiffer S., Benkovic S.J. Coupled motions in enzyme catalysis. Curr. Opin. Chem. Biol. 2010, 14:644-651.
23. Jansen A.J., Josefsson E.C., Rumjantseva V., Liu Q.P., Falet H., Bergmeier W., Cifuni S.M., Sackstein R., von Andrian U.H., Wagner D.D., Hartwig J.H., Hoffmeister K.M. Desialylation accelerates platelet clearance following refrigeration and initiates GPIbα metalloproteinase-mediated cleavage in mice. Blood 2012, 119:1263-1273.