Multiple processing of Ig-Hepta/GPR116, a G protein-coupled receptor with immunoglobulin (Ig)-like repeats, and generation of EGF2-like fragment

Journal of Biochemistry

Volumn 140, Issue 3, 2006, Pages 445-452

  Fukuzawa, Taku ^a   Hirose, Shigehisa ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

Furin; G protein coupled receptor; LNB TM7; Proteolytic processing; SEA module

Indexed keywords

AGRIN; AMINO ACID; CADHERIN; CELL SURFACE RECEPTOR; ENTEROPEPTIDASE; EPIDERMAL GROWTH FACTOR; FURIN; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; IMMUNOGLOBULIN; LECTIN; PROTEIN IG HEPTA; THROMBOSPONDIN; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANTIBODY PRODUCTION; ARTICLE; BETA CHAIN; CONTROLLED STUDY; EXPERIMENTAL MODEL; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; MICROARRAY ANALYSIS; NONHUMAN; NORTHERN BLOTTING; PLASMID; PROTEIN DEGRADATION; RAT; WESTERN BLOTTING;

ANIMALS; BLOTTING, NORTHERN; BLOTTING, WESTERN; CELL LINE; DNA PRIMERS; FURIN; GENETIC VECTORS; HUMANS; IMMUNOPRECIPITATION; MICROARRAY ANALYSIS; MITOCHONDRIAL PROTEINS; PEPTIDE ELONGATION FACTOR G; PROTEIN PROCESSING, POST-TRANSLATIONAL; RATS; RECEPTORS, G-PROTEIN-COUPLED; TRANSFECTION;

EID: 33750719111     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj170     Document Type: Article

References (28)

1. Stacey, M., Lin, H.H., Gordon, S., and McKnight, A.J. (2000) LNB-TM7, a group of seven-transmembrane proteins related to family-B G-protein-coupled receptors. Trends Biochem Sci. 25, 284-289
2. Fredriksson, R., Lagerstrom, M.C., Hoglund, P.J., and Schioth, H.B. (2002) Novel human G protein-coupled receptors with long N-terminals containing GPS domains and Ser/Thr-rich regions. FEBS Lett. 531, 407-114
3. Fredriksson, R., Gloriam, D.E., Hoglund, P.J., Lagerstrom, M.C., and Schioth, H.B. (2003) There exist at least 30 human G-protein-coupled receptors with long Ser/Thr-rich N-termini. Biochem Blophys. Res. Commun. 301, 725-734
4. Curtin, J.A., Quint, E., Tsipouri, V., Arkell, R.M., Cattanach, B., Copp, A. J., Henderson, D. J., Spurr, N., Stanier, P., Fisher, E.M., Nolan, P.M., Steel, K.P., Brown, S.D., Gray, I.C., and Murdoch, J.N. (2003) Mutation of Celsr1 disrupts planar polarity of inner ear hair cells and causes severe neural tube defects in the mouse. Curr. Biol. 13, 1129-1133
5. Kaur, B., Brat, D.J., Devi, N.S., and Van Meir, E.G. (2005) Vasculostatin, a proteolytic fragment of brain angiogenesis inhibitor 1, is an antiangiogenic and antitumorigenic factor. Oncogens 24, 3632-3642
6. Stacey, M., Chang, G.W., Davies, J.Q., Kwakkenbos, M.J., Sanderson, R.D., Hamann, J., Gordon, S., and Lin, H.H. (2003) The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans. Blood 102, 2916-2924
7. Leemans, J.C., te Velde, A.A., Plorquin, S., Bennink, R.J., de Bruin, K., van Lier, R.A., van der, P.T., and Hamann, J. (2004) The epidermal growth factor-seven transmembrane (EGF-TM7) receptor CD97 is required for neutrophil migration and host defense. J. Immunol. 172, 1125-1131
8. Sugita, S., Ichtchenko, K., Khvotchev, M., and Sudhof, T.C. (1998) alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual family of ubiquitous G-protein-linked receptors. G-protein coupling not required for triggering exocytosis. J. Biol. Chem. 273, 32715-32724
9. Abe, J., Fukuzawa, T., and Hirose, S. (2002) Cleavage of Ig-Hepta at a "SEA" module and at a conserved G protein-coupled receptor proteolytic site. J. Biol. Chem. 277, 23391-23398
10. Bork, P. and Patthy, L. (1995) The SEA module: a new extracellular domain associated with O-glycosylation. Protein Sci. 4, 1421-1425
11. Baruch, A., Hartmann, M., Yoeli, M., Adereth, Y., Greenstein, S., Stadler, Y., Skornik, Y., Zaretsky, J., Smorodinsky, N.I., Keydar, L, and Wreschner, D.H. (1999) The breast cancer-associated MUC1 gene generates both a receptor and its cognate binding protein. Cancer Res. 59, 1552-1561
12. Khatri, I.A., Wang, R., and Forstner, J.F. (2004) Evidence for a second peptide cleavage in the C-terminal domain of rodent intestinal mucin Muc3. Biochem. J. 378, 207-212
13. Wreschner, D.H., McGuckin, M.A., Williams, S.J., Baruch, A., Yoeli, M., Ziv, R., Okun, L., Zaretsky, J., Smorodinsky, N., Keydar, I., Neophytou, P., Stacey, M., Lin, H.H., and Gordon, S. (2002) Generation of ligand-receptor alliances by "SEA" module-mediated cleavage of membrane-associated mucin proteins. Protein Sci. 11, 698-706
14. Nakayama, K. (1997) Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327 (Pt 3), 625-635
15. Hadano, S., Otomo, A., Suzuki-Utsunomiya, K., Kunita, R., Yanagisawa, Y., Showguchi-Miyata, J., Mizumura, H., and Ikeda, J.E. (2004) ALS2CL, the novel protein highly homologous to the carboxy-terminal half of ALS2, binds to Rab5 and modulates endosome dynamics. FEBS Lett. 575, 64-70
16. Nakamura, N., Fukuda, H., Kato, A., and Hirose, S. (2005) MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking. Mol. Biol. Cell 16, 1696-1710
17. Carraway, K.L., III, Rossi, E.A., Komatsu, M., Price-Schiavi, S.A., Huang, D., Guy, P.M., Carvajal, M.E., Fregien, N., Carraway, C.A., and Carraway, K.L. (1999) An intramembrane modulator of the ErbB2 receptor tyrosine kinase that potentiates neuregulin signaling. J. Biol. Chem. 274, 5263-5266
18. Julian, J. and Carson, D.D. (2002) Formation of MUC1 metabolic complex is conserved in tumor-derived and normal epithelial cells. Biochem. Biophys. Res. Commun. 293, 1183-1190
19. McNeer, R.R., Huang, D., Fregien, N.L., and Carraway, K.L. (1998) Sialomucin complex in the rat respiratory tract: a model for its role in epithelial protection. Biochem. J. 330 (Pt 2), 737-744
20. Schroeder, J.A., Thompson, M.C., Gardner, M.M., and Gendler, S.J. (2001) Transgenic MUC1 interacts with epidermal growth factor receptor and correlates with mitogen-activated protein kinase activation in the mouse mammary gland. J. Biol. Chem. 276, 13057-13064
21. Abe, J., Suzuki, H., Notoya, M., Yamamoto, T., and Hirose, S. (1999) Ig-Hepta, a novel member of the G protein-coupled hepta-helical receptor (GPCR) family that has immunoglobulin-like repeats in a long N-terminal extracellular domain and defines a new subfamily of GPCRs. J. Biol. Chem. 274, 19957-19964
22. Lin, H.H., Chang, G.W., Davies, J.Q., Stacey, M., Harris, J., and Gordon, S. (2004) Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif. J. Biol. Chem. 279, 31823-31832
23. Krasnoperov, V., Lu, Y., Buryanovsky, L., Neubert, T.A., Ichtchenko, K., and Petrenko, A.G. (2002) Post-translational proteolytic processing of the calcium-independent receptor of alpha-latrotoxin (CIRL), a natural chimera of the cell adhesion protein and the G protein-coupled receptor. Role of the G protein-coupled receptor proteolysis site (GPS) motif. J. Biol. Chem. 277, 46518-46526
24. Qian, F., Boletta, A., Bhunia, A.K., Xu, H., Liu, L., Ahrabi, A.K., Watnick, T.J., Zhou, F., and Germino, G.G. (2002) Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations. Proc. Natl. Acad. Sci. USA 99, 16981-16986
25. Levitin, F., Stern, O., Weiss, M., Gil-Henn, C., Ziv, R., Prokocimer, Z., Smorodinsky, N.I., Rubinstein, D.B., and Wreschner, D.H. (2005) The MUC1 SEA module is a self-cleaving domain. J. Biol. Chem. 280, 33374-33386
26. Macao, B., Johansson, D.G., Hansson, G.G., and Hard, T. (2006) Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin. Nat. Struct. Mol. Biol. 13, 71-76
27. Steiner, D.F., Smeekens, S.P., Ohagi, S., and Chan, S. J. (1992) The new enzymology of precursor processing endoproteases. J. Biol. Chem. 267, 23435-23438
28. Nakayama, K, Kim, W.S., Torii, S., Hosaka, M., Nakagawa, T., Ikemizu, J., Baba, T., and Murakami, K. (1992) Identification of the fourth member of the mammalian endoprotease family homologous to the yeast Kex2 protease. Its testis-specific expression. J. Biol. Chem. 267, 5897-5900