메뉴 건너뛰기




Volumn 706, Issue , 2010, Pages 49-58

GPS proteolytic cleavage of adhesion-GPCRs

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LATROTOXIN; CD97 ANTIGEN; CELL SURFACE RECEPTOR; CYSTEINE; G PROTEIN COUPLED RECEPTOR; LACTROPHILIN; LEUCINE; POLYCYSTIN 1; SERINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 79960775391     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-7913-1_4     Document Type: Article
Times cited : (28)

References (41)
  • 1
    • 0034213071 scopus 로고    scopus 로고
    • LNB-TM7, a group of seven-transmembrane proteins related to family-B G-protein-coupled receptors
    • DOI 10.1016/S0968-0004(00)01583-8, PII S0968000400015838
    • Stacey M, Lin HH, Gordon S et al. LNB-TM7, a group of seven-transmembrane proteins related to family-B G-protein-coupled receptors. Trends Biochem Sci 2000; 25(6):284-289. (Pubitemid 30333387)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.6 , pp. 284-289
    • Stacey, M.1    Lin, H.-H.2    Gordon, S.3    McKnight, A.J.4
  • 2
    • 53149135394 scopus 로고    scopus 로고
    • Adhesion-GPCRs: Emerging roles for novel receptors
    • Yona S, Lin HH, Siu WO et al. Adhesion-GPCRs: Emerging roles for novel receptors. Trends Biochem Sci 2008;33(10):491-500.
    • (2008) Trends Biochem Sci , vol.33 , Issue.10 , pp. 491-500
    • Yona, S.1    Lin, H.H.2    Siu, W.O.3
  • 3
    • 0033525112 scopus 로고    scopus 로고
    • Structural requirements for α-latrotoxin binding and α-latrotoxin- stimulated secretion: A study with calcium-independent receptor of α- latrotoxin (CIRL) deletion mutants
    • DOI 10.1074/jbc.274.6.3590
    • Krasnoperov V, Bittner MA, Holz RW et al. Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-stimulated secretion. A study with calcium-independent receptor of alpha-latrotoxin (CIRL) deletion mutants. J Biol Chem 1999; 274(6):3590-3596. (Pubitemid 29077201)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.6 , pp. 3590-3596
    • Krasnoperov, V.1    Bittner, M.A.2    Holz, R.W.3    Chepurny, O.4    Petrenko, A.G.5
  • 5
    • 35248884458 scopus 로고    scopus 로고
    • The Adhesion GPCRs: A unique family of G protein-coupled receptors with important roles in both central and peripheral tissues
    • DOI 10.1007/s00018-007-7067-1
    • Bjarnadottir TK, Fredriksson R, Schioth HB. The adhesion GPCRs: A unique family of G protein-coupled receptors with important roles in both central and peripheral tissues. Cell Mol Life Sci 2007; 64(16):2104-2119. (Pubitemid 350092419)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.16 , pp. 2104-2119
    • Bjarnadottir, T.K.1    Fredriksson, R.2    Schioth, H.B.3
  • 6
    • 3843101589 scopus 로고    scopus 로고
    • Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif
    • DOI 10.1074/jbc.M402974200
    • Lin HH, Chang GW, Davies JQ et al. Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif. J Biol Chem 2004; 279(30):31823-31832. (Pubitemid 39037855)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.30 , pp. 31823-31832
    • Lin, H.-H.1    Chang, G.-W.2    Davies, J.Q.3    Stacey, M.4    Harris, J.5    Gordon, S.6
  • 7
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • Brannigan JA, Dodson G, Duggleby HJ et al. A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 1995; 378(6555):416-419.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 416-419
    • Brannigan, J.A.1    Dodson, G.2    Duggleby, H.J.3
  • 8
    • 0031970649 scopus 로고    scopus 로고
    • Breaking up is easy with esters
    • DOI 10.1038/nsb0498-249
    • Perler FB. Breaking up is easy with esters. Nat Struct Biol 1998; 5(4):249-252. (Pubitemid 28164871)
    • (1998) Nature Structural Biology , vol.5 , Issue.4 , pp. 249-252
    • Perler, F.B.1
  • 10
    • 0037195853 scopus 로고    scopus 로고
    • Post-translational proteolytic processing of the calcium-independent receptor of α-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
    • DOI 10.1074/jbc.M206415200
    • Krasnoperov V, Lu Y, Buryanovsky L et al. 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 2002; 277(48):46518-46526. (Pubitemid 35417649)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46518-46526
    • Krasnoperov, V.1    Lu, Y.2    Buryanovsky, L.3    Neubert, T.A.4    Ichtehenko, K.5    Petrenko, A.G.6
  • 14
    • 0037059813 scopus 로고    scopus 로고
    • SuREJ3, a polycystin-1 protein, is cleaved at the GPS domain and localizes to the acrosomal region of sea urchin sperm
    • DOI 10.1074/jbc.M109673200
    • Mengerink KJ, Moy GW, Vacquier VD. suREJ3, a polycystin-1 protein, is cleaved at the GPS domain and localizes to the acrosomal region of sea urchin sperm. J Biol Chem 2002; 277(2):943-948. (Pubitemid 34968838)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 943-948
    • Mengerink, K.J.1    Moy, G.W.2    Vacquier, V.D.3
  • 15
    • 0029977293 scopus 로고    scopus 로고
    • The sea urchin sperm receptor for egg jelly is a modular protein with extensive homology to the human polycystic kidney disease protein, PKD1
    • DOI 10.1083/jcb.133.4.809
    • Moy GW, Mendoza LM, Schulz JR et al. The sea urchin sperm receptor for egg jelly is a modular protein with extensive homology to the human polycystic kidney disease protein, PKD1. J Cell Biol 1996; 133(4):809-817. (Pubitemid 26160983)
    • (1996) Journal of Cell Biology , vol.133 , Issue.4 , pp. 809-817
    • Moy, G.W.1    Mendoza, L.M.2    Schulz, J.R.3    Swanson, W.J.4    Glabe, C.G.5    Vacquier, V.D.6
  • 18
    • 0037189505 scopus 로고    scopus 로고
    • Cleavage of Ig-Hepta at a 'SEA' module and at a conserved G protein-coupled receptor proteolytic site
    • DOI 10.1074/jbc.M110877200
    • Abe J, Fukuzawa T, Hirose S. Cleavage of Ig-Hepta at a "SEA" module and at a conserved G protein-coupled receptor proteolytic site. J Biol Chem 2002; 277(26):23391-23398. (Pubitemid 34952170)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23391-23398
    • Abe, J.1    Fukuzawa, T.2    Hirose, S.3
  • 19
    • 70349472909 scopus 로고    scopus 로고
    • Site-specific N-glycosylation regulates the GPS auto-proteolysis of CD97
    • Hsiao CC, Cheng KF, Chen HY et al. Site-specific N-glycosylation regulates the GPS auto-proteolysis of CD97. FEBS Lett 2009; 583(19):3285-3290.
    • (2009) FEBS Lett , vol.583 , Issue.19 , pp. 3285-3290
    • Hsiao, C.C.1    Cheng, K.F.2    Chen, H.Y.3
  • 22
    • 0035830870 scopus 로고    scopus 로고
    • ETL, anovel seven-transmembrane receptor that is developmentally regulated in the heart. ETL is a member of the secretin family and belongs to the epidermal growth factor-seven-transmembrane subfamily
    • Nechiporuk T, Urness LD, Keating MT. ETL, anovel seven-transmembrane receptor that is developmentally regulated in the heart. ETL is a member of the secretin family and belongs to the epidermal growth factor-seven-transmembrane subfamily. J Biol Chem 2001; 276(6):4150-4157.
    • (2001) J Biol Chem , vol.276 , Issue.6 , pp. 4150-4157
    • Nechiporuk, T.1    Urness, L.D.2    Keating, M.T.3
  • 24
    • 0037047359 scopus 로고    scopus 로고
    • EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B-lymphoma cell line A20
    • Stacey M, Chang GW, Sanos SL et al. EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in activated mouse macrophages, binds to a putative cellular ligand on B-lymphoma cell line A20. J Biol Chem 2002; 277(32):29283-29293.
    • (2002) J Biol Chem , vol.277 , Issue.32 , pp. 29283-29293
    • Stacey, M.1    Chang, G.W.2    Sanos, S.L.3
  • 25
    • 34547580803 scopus 로고    scopus 로고
    • Characterization of cis-autoproteolysis of polycystin-1, the product of human polycystic kidney disease 1 gene
    • DOI 10.1074/jbc.M703218200
    • Wei W, Hackmann K, Xu H et al. Characterization of cis-autoproteolysis of polycystin-1, the product of human polycystic kidney disease 1 gene. J Biol Chem 2007; 282(30):21729-21737. (Pubitemid 47195735)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.30 , pp. 21729-21737
    • Wei, W.1    Hackmann, K.2    Xu, H.3    Germino, G.4    Qian, F.5
  • 27
    • 3042772969 scopus 로고    scopus 로고
    • DREG, a developmentally regulated G protein-coupled receptor containing two conserved proteolytic cleavage sites
    • DOI 10.1111/j.1356-9597.2004.00743.x
    • Moriguchi T, Haraguchi K, Ueda N et al. DREG, a developmentally regulated G protein-coupled receptor containing two conserved proteolytic cleavage sites. Genes Cells 2004; 9(6):549-560. (Pubitemid 38877784)
    • (2004) Genes to Cells , vol.9 , Issue.6 , pp. 549-560
    • Moriguchi, T.1    Haraguchi, K.2    Ueda, N.3    Okada, M.4    Furuya, T.5    Akiyama, T.6
  • 28
    • 33845962038 scopus 로고    scopus 로고
    • 3 to glycosaminoglycans
    • DOI 10.1074/jbc.M605291200
    • Vallon M, Essler M. Proteolytically processed soluble tumor endothelial marker (TEM) 5 mediates endothelial cell survival during angiogenesis by linking integrin alpha(v)beta3 to glycosaminoglycans. J Biol Chem 2006; 281(45):34179-34188. (Pubitemid 46036626)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34179-34188
    • Vallon, M.1    Essler, M.2
  • 29
    • 0033051821 scopus 로고    scopus 로고
    • Identification of a human homologue of the sea urchin receptor for egg jelly: A polycystic kidney disease-like protein
    • Hughes J, Ward CJ, Aspinwall R et al. Identification of a human homologue of the sea urchin receptor for egg jelly: A polycystic kidney disease-like protein. Hum Mol Genet 1999; 8(3):543-549. (Pubitemid 29097343)
    • (1999) Human Molecular Genetics , vol.8 , Issue.3 , pp. 543-549
    • Hughes, J.1    Ward, C.J.2    Aspinwall, R.3    Butler, R.4    Harris, P.C.5
  • 31
    • 0028641336 scopus 로고
    • Autoproteolysis in hedgehog protein biogenesis
    • Lee JJ, Ekker SC, von Kessler DP et al. Autoproteolysis in hedgehog protein biogenesis. Science 1994; 266(5190):1528-1537.
    • (1994) Science , vol.266 , Issue.5190 , pp. 1528-1537
    • Lee, J.J.1    Ekker, S.C.2    Von Kessler, D.P.3
  • 32
    • 0028948811 scopus 로고
    • The product of hedgehog autoproteolytic cleavage active in local and long-range signalling
    • Porter JA, von Kessler DP, Ekker SC et al. The product of hedgehog autoproteolytic cleavage active in local and long-range signalling. Nature 1995; 374(6520):363-366.
    • (1995) Nature , vol.374 , Issue.6520 , pp. 363-366
    • Porter, J.A.1    Von Kessler, D.P.2    Ekker, S.C.3
  • 33
    • 0030051163 scopus 로고    scopus 로고
    • Activation of glycosylasparaginase. Formation of active N-terminal threonine by intramolecular autoproteolysis
    • Guan C, Cui T, Rao V et al. Activation of glycosylasparaginase. Formation of active N-terminal threonine by intramolecular autoproteolysis. J Biol Chem 1996; 271(3):1732-1737.
    • (1996) J Biol Chem , vol.271 , Issue.3 , pp. 1732-1737
    • Guan, C.1    Cui, T.2    Rao, V.3
  • 34
    • 0028786346 scopus 로고
    • Three-dimensional structure of human lysosomal aspartylglucosaminidase
    • Oinonen C, Tikkanen R, Rouvinen J et al. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nat Struct Biol 1995; 2(12): 1102-1108.
    • (1995) Nat Struct Biol , vol.2 , Issue.12 , pp. 1102-1108
    • Oinonen, C.1    Tikkanen, R.2    Rouvinen, J.3
  • 35
    • 0029936212 scopus 로고    scopus 로고
    • Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: Implications for catalytic mechanism and autocatalytic activation
    • Tikkanen R, Riikonen A, Oinonen C et al. Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: Implications for catalytic mechanism and autocatalytic activation. EMBO J 1996; 15(12):2954-2960. (Pubitemid 26187743)
    • (1996) EMBO Journal , vol.15 , Issue.12 , pp. 2954-2960
    • Tikkanen, R.1    Riikonen, A.2    Oinonen, C.3    Rouvinen, J.4    Peltonen, L.5
  • 36
    • 0033520327 scopus 로고    scopus 로고
    • Structural insights into the mechanism of intramolecular proteolysis
    • DOI 10.1016/S0092-8674(00)80052-5
    • Xu Q, Buckley D, Guan C et al. Structural insights into the mechanism of intramolecular proteolysis. Cell 1999; 98(5):651-661. (Pubitemid 29418956)
    • (1999) Cell , vol.98 , Issue.5 , pp. 651-661
    • Xu, Q.1    Buckley, D.2    Guan, C.3    Guo, H.-C.4
  • 38
    • 47249103800 scopus 로고    scopus 로고
    • Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a G alpha 12/13 and Rho pathway
    • Iguchi T, Sakata K, Yoshizaki K et al. Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell migration via a G alpha 12/13 and Rho pathway. J Biol Chem 2008; 283(21):14469-14478.
    • (2008) J Biol Chem , vol.283 , Issue.21 , pp. 14469-14478
    • Iguchi, T.1    Sakata, K.2    Yoshizaki, K.3
  • 39
    • 0038642821 scopus 로고    scopus 로고
    • Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif
    • DOI 10.1016/S0014-5793(03)00695-1
    • Chang GW, Stacey M, Kwakkenbos MJ et al. Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif. FEBS Lett 2003; 547(1-3): 145-150. (Pubitemid 36829395)
    • (2003) FEBS Letters , vol.547 , Issue.1-3 , pp. 145-150
    • Chang, G.-W.1    Stacey, M.2    Kwakkenbos, M.J.3    Hamann, J.4    Gordon, S.5    Lin, H.-H.6
  • 41
    • 65249085110 scopus 로고    scopus 로고
    • Functional cross-interaction of the fragments produced by the cleavage of distinct adhesion G-protein-coupled receptors
    • Silva JP, Lelianova V, Hopkins C et al. Functional cross-interaction of the fragments produced by the cleavage of distinct adhesion G-protein-coupled receptors. J Biol Chem 2009; 284(10):6495-6506.
    • (2009) J Biol Chem , vol.284 , Issue.10 , pp. 6495-6506
    • Silva, J.P.1    Lelianova, V.2    Hopkins, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.