메뉴 건너뛰기




Volumn 307, Issue 1, 2005, Pages 65-75

Cysteine residues are critical for chemokine receptor CXCR2 functional properties

Author keywords

Chemotaxis; CXCR2; Cysteines; Receptor dimerization; Signal transduction

Indexed keywords

CHEMOKINE RECEPTOR CXCR2; CYSTEINE; DIMER; INTERLEUKIN 8; MONOMER;

EID: 19544368784     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.02.020     Document Type: Article
Times cited : (15)

References (32)
  • 2
    • 0031570454 scopus 로고    scopus 로고
    • The differential ability of IL-8 and neutrophil-activating peptide-2 to induce attenuation of chemotaxis is mediated by their divergent capabilities to phosphorylate CXCR2 (IL-8 receptor B)
    • A. Ben-Baruch, M. Grimm, K. Bengali, G.A. Evans, O. Chertov, J.M. Wang, O.M. Howard, N. Mukaida, K. Matsushima, and J.J. Oppenheim The differential ability of IL-8 and neutrophil-activating peptide-2 to induce attenuation of chemotaxis is mediated by their divergent capabilities to phosphorylate CXCR2 (IL-8 receptor B) J. Immunol. 158 1997 5927 5933
    • (1997) J. Immunol. , vol.158 , pp. 5927-5933
    • Ben-Baruch, A.1    Grimm, M.2    Bengali, K.3    Evans, G.A.4    Chertov, O.5    Wang, J.M.6    Howard, O.M.7    Mukaida, N.8    Matsushima, K.9    Oppenheim, J.J.10
  • 3
    • 0030887899 scopus 로고    scopus 로고
    • IL-8 and NAP-2 differ in their capacities to bind and chemoattract 293 cells transfected with either IL-8 receptor type a or type B
    • A. Ben-Baruch, K. Bengali, K. Tani, L. Xu, J.J. Oppenheim, and J.M. Wang IL-8 and NAP-2 differ in their capacities to bind and chemoattract 293 cells transfected with either IL-8 receptor type A or type B Cytokine 9 1997 37 45
    • (1997) Cytokine , vol.9 , pp. 37-45
    • Ben-Baruch, A.1    Bengali, K.2    Tani, K.3    Xu, L.4    Oppenheim, J.J.5    Wang, J.M.6
  • 4
    • 0033384911 scopus 로고    scopus 로고
    • Differential modes of regulation of CXC chemokine-induced internalization and recycling of human CXCR1 and CXCR2
    • R. Feniger-Barish, M. Ran, A. Zaslaver, and A. Ben-Baruch Differential modes of regulation of CXC chemokine-induced internalization and recycling of human CXCR1 and CXCR2 Cytokine 11 1999 996 1009
    • (1999) Cytokine , vol.11 , pp. 996-1009
    • Feniger-Barish, R.1    Ran, M.2    Zaslaver, A.3    Ben-Baruch, A.4
  • 5
    • 0034608742 scopus 로고    scopus 로고
    • Expression of CX3CR1 chemokine receptors on neurons and their role in neuronal survival
    • O. Meucci, A. Fatatis, A.A. Simen, and R.J. Miller Expression of CX3CR1 chemokine receptors on neurons and their role in neuronal survival Proc. Natl. Acad. Sci. U. S. A. 97 1998 8075 8080
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8075-8080
    • Meucci, O.1    Fatatis, A.2    Simen, A.A.3    Miller, R.J.4
  • 7
    • 0032414498 scopus 로고    scopus 로고
    • CXC chemokines interleukin-8 (IL-8) and growth-related gene product alpha (GRO alpha) modulate Purkinje neuron activity in mouse cerebellum
    • A. Giovannelli, C. Limatola, D. Ragozzino, A.M. Mileo, M.T. Ciotti, D. Mercanti, A. Santoni, and F. Eusebi CXC chemokines interleukin-8 (IL-8) and growth-related gene product alpha (GRO alpha) modulate Purkinje neuron activity in mouse cerebellum J. Neuroimmunol. 92 1998 122 132
    • (1998) J. Neuroimmunol. , vol.92 , pp. 122-132
    • Giovannelli, A.1    Limatola, C.2    Ragozzino, D.3    Mileo, A.M.4    Ciotti, M.T.5    Mercanti, D.6    Santoni, A.7    Eusebi, F.8
  • 8
    • 0034839338 scopus 로고    scopus 로고
    • 2+ currents in identified cholinergic septal neurons expressing CXCR1 and CXCR2 receptor mRNAs
    • 2+ currents in identified cholinergic septal neurons expressing CXCR1 and CXCR2 receptor mRNAs J. Neurochem. 78 2001 960 971
    • (2001) J. Neurochem. , vol.78 , pp. 960-971
    • Puma, C.1    Danik, M.2    Quirion, R.3    Ramon, F.4    Williams, S.5
  • 11
    • 0035907361 scopus 로고    scopus 로고
    • Phosphorylation-independent association of CXCR2 with the protein phosphatase 2A core enzyme
    • G.H. Fan, W. Yang, J. Sai, and A. Richmond Phosphorylation-independent association of CXCR2 with the protein phosphatase 2A core enzyme J. Biol. Chem. 276 2001 16960 16968
    • (2001) J. Biol. Chem. , vol.276 , pp. 16960-16968
    • Fan, G.H.1    Yang, W.2    Sai, J.3    Richmond, A.4
  • 12
    • 0035936552 scopus 로고    scopus 로고
    • Identification of a motif in the carboxyl terminus of CXCR2 that is involved in adaptin 2 binding and receptor internalization
    • G.H. Fan, W. Yang, X.J. Wang, Q. Qian, and A. Richmond Identification of a motif in the carboxyl terminus of CXCR2 that is involved in adaptin 2 binding and receptor internalization Biochemistry 40 2001 791 800
    • (2001) Biochemistry , vol.40 , pp. 791-800
    • Fan, G.H.1    Yang, W.2    Wang, X.J.3    Qian, Q.4    Richmond, A.5
  • 13
    • 0037155284 scopus 로고    scopus 로고
    • Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking
    • G.H. Fan, W. Yang, J. Sai, and A. Richmond Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking J. Biol. Chem. 277 2002 6590 6597
    • (2002) J. Biol. Chem. , vol.277 , pp. 6590-6597
    • Fan, G.H.1    Yang, W.2    Sai, J.3    Richmond, A.4
  • 14
    • 0037443490 scopus 로고    scopus 로고
    • Role of the cytoplasmic tails of CXCR1 and CXCR2 in mediating leukocyte migration, activation, and regulation
    • R.M. Richardson, R.J. Marjoram, L.S. Barak, and R. Snyderman Role of the cytoplasmic tails of CXCR1 and CXCR2 in mediating leukocyte migration, activation, and regulation J. Immunol. 170 2003 2904 2911
    • (2003) J. Immunol. , vol.170 , pp. 2904-2911
    • Richardson, R.M.1    Marjoram, R.J.2    Barak, L.S.3    Snyderman, R.4
  • 18
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the delta opioid receptor: Implication for a role in receptor internalization
    • S. Cvejic, and L.A. Devi Dimerization of the delta opioid receptor: implication for a role in receptor internalization J. Biol. Chem. 272 1997 26959 26964
    • (1997) J. Biol. Chem. , vol.272 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 19
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • B.A. Jordan, and L.A. Devi G-protein-coupled receptor heterodimerization modulates receptor function Nature 399 1999 697 700
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 20
    • 0034602293 scopus 로고    scopus 로고
    • Cys-140 is critical for metabotropic glutamate receptor-1 dimerization
    • K. Ray, and B.C. Hauschild Cys-140 is critical for metabotropic glutamate receptor-1 dimerization J. Biol. Chem. 275 2000 34245 34251
    • (2000) J. Biol. Chem. , vol.275 , pp. 34245-34251
    • Ray, K.1    Hauschild, B.C.2
  • 22
    • 0035895907 scopus 로고    scopus 로고
    • The extracellular calcium-sensing receptor dimerizes through multiple types of intermolecular interactions
    • Z. Zhang, S. Sun, S.J. Quinn, E.M. Brown, and M. Bai The extracellular calcium-sensing receptor dimerizes through multiple types of intermolecular interactions J. Biol. Chem. 276 2001 5316 5322
    • (2001) J. Biol. Chem. , vol.276 , pp. 5316-5322
    • Zhang, Z.1    Sun, S.2    Quinn, S.J.3    Brown, E.M.4    Bai, M.5
  • 23
    • 0035955633 scopus 로고    scopus 로고
    • A membrane-proximal basic domain and cysteine cluster in the C-terminal tail of CCR5 constitute a bipartite motif critical for cell surface expression
    • S. Venkatesan, A. Petrovic, M. Locati, Y.O. Kim, D. Weissman, and P.M. Murphy A membrane-proximal basic domain and cysteine cluster in the C-terminal tail of CCR5 constitute a bipartite motif critical for cell surface expression J. Biol. Chem. 276 2001 40133 40145
    • (2001) J. Biol. Chem. , vol.276 , pp. 40133-40145
    • Venkatesan, S.1    Petrovic, A.2    Locati, M.3    Kim, Y.O.4    Weissman, D.5    Murphy, P.M.6
  • 24
    • 0037008084 scopus 로고    scopus 로고
    • Mutating the four extracellular cysteines in the chemokine receptor CCR6 reveals their differing roles in receptor trafficking, ligand binding, and signaling
    • L.S. Ai, and F. Liao Mutating the four extracellular cysteines in the chemokine receptor CCR6 reveals their differing roles in receptor trafficking, ligand binding, and signaling Biochemistry 41 2002 8332 8341
    • (2002) Biochemistry , vol.41 , pp. 8332-8341
    • Ai, L.S.1    Liao, F.2
  • 25
    • 0242572132 scopus 로고    scopus 로고
    • Dimerization of G-protein-coupled receptors: Roles in signal transduction
    • M. Bai Dimerization of G-protein-coupled receptors: roles in signal transduction Cell Signalling 16 2004 175 186
    • (2004) Cell Signalling , vol.16 , pp. 175-186
    • Bai, M.1
  • 26
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • S. Terrillon, and M. Bouvier Roles of G-protein-coupled receptor dimerization EMBO Rep. 5 2004 30 34
    • (2004) EMBO Rep. , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 28
    • 0242289624 scopus 로고    scopus 로고
    • Homo- and hetero-oligomerization of G protein-coupled receptors
    • S.P. Lee, B.F. O'Dowd, and S.R. George Homo- and hetero-oligomerization of G protein-coupled receptors Life Sci. 74 2003 173 180
    • (2003) Life Sci. , vol.74 , pp. 173-180
    • Lee, S.P.1    O'Dowd, B.F.2    George, S.R.3
  • 30
    • 0242535121 scopus 로고    scopus 로고
    • The role of conserved extracellular cysteine residues in vasopressin V2 receptor function and properties of two naturally occurring mutant receptors with additional extracellular cysteine residues
    • R. Schülein, K. Zuhlke, A. Oksche, R. Hermosilla, J. Furkert, and W. Rosenthal The role of conserved extracellular cysteine residues in vasopressin V2 receptor function and properties of two naturally occurring mutant receptors with additional extracellular cysteine residues FEBS Lett. 466 2000 101 106
    • (2000) FEBS Lett. , vol.466 , pp. 101-106
    • Schülein, R.1    Zuhlke, K.2    Oksche, A.3    Hermosilla, R.4    Furkert, J.5    Rosenthal, W.6
  • 31
    • 0141431029 scopus 로고    scopus 로고
    • D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4
    • S.P. Lee, B.F. O'Dowd, R.D. Rajaram, T. Nguyen, and S.R. George D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4 Biochemistry 42 2003 11023 11031
    • (2003) Biochemistry , vol.42 , pp. 11023-11031
    • Lee, S.P.1    O'Dowd, B.F.2    Rajaram, R.D.3    Nguyen, T.4    George, S.R.5
  • 32
    • 0032847878 scopus 로고    scopus 로고
    • Mutation of human μ opioid receptor extracellular "disulfide cysteine" residues alters ligand binding but does not prevent receptor targeting to the cell plasma membrane
    • P. Zhang, P.S. Johnson, C. Zollner, W. Wang, Z. Wang, A.E. Montes, B.K. Seidleck, C.J. Blaschak, and C.K. Surratt Mutation of human μ opioid receptor extracellular "disulfide cysteine" residues alters ligand binding but does not prevent receptor targeting to the cell plasma membrane Mol. Brain Res. 72 1999 195 204
    • (1999) Mol. Brain Res. , vol.72 , pp. 195-204
    • Zhang, P.1    Johnson, P.S.2    Zollner, C.3    Wang, W.4    Wang, Z.5    Montes, A.E.6    Seidleck, B.K.7    Blaschak, C.J.8    Surratt, C.K.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.