메뉴 건너뛰기




Volumn 468, Issue 3, 2015, Pages 495-506

Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes

Author keywords

Growth hormone receptor; Immuno t cell receptor activation motifs; Intrinsically disordered protein; Membrane interaction; Prolactin receptor; Signalling

Indexed keywords

1 PALMITOYL 2 OLEOYL GLYCERO 3 PHOSPHOSERINE; 2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; CYTOKINE RECEPTOR; GROWTH HORMONE RECEPTOR; INTRINSICALLY DISORDERED PROTEIN; JANUS KINASE 2; LIPID; MEMBRANE LIPID; PROLACTIN RECEPTOR; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG; 1-PALMITOYL-2-OLEOYLGLYCERO-3-PHOSPHOSERINE; 1-PALMITOYL-2-OLEOYLPHOSPHATIDYLCHOLINE; LIPID BILAYER; PEPTIDE FRAGMENT; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; RECOMBINANT PROTEIN; TYROSINE;

EID: 84934905479     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141243     Document Type: Article
Times cited : (68)

References (66)
  • 1
    • 0032460226 scopus 로고    scopus 로고
    • Prolactin (PRL) and its receptor: Actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice
    • CrossRef PubMed
    • Bole-Feysot, C., Goffin, V., Edery, M., Binart, N. and Kelly, P.A. (1998) Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice. Endocr. Rev. 19, 225-268 CrossRef PubMed
    • (1998) Endocr. Rev. , vol.19 , pp. 225-268
    • Bole-Feysot, C.1    Goffin, V.2    Edery, M.3    Binart, N.4    Kelly, P.A.5
  • 2
    • 77955921088 scopus 로고    scopus 로고
    • The growth hormone receptor: Mechanism of activation and clinical implications
    • CrossRef PubMed
    • Brooks, A.J. and Waters, M.J. (2010) The growth hormone receptor: mechanism of activation and clinical implications. Nat. Rev. Endocrinol. 6, 515-525 CrossRef PubMed
    • (2010) Nat. Rev. Endocrinol. , vol.6 , pp. 515-525
    • Brooks, A.J.1    Waters, M.J.2
  • 3
    • 34548329392 scopus 로고    scopus 로고
    • Evolution of class I cytokine receptors
    • CrossRef PubMed
    • Liongue, C. and Ward, A.C. (2007) Evolution of class I cytokine receptors. BMC Evol. Biol. 7, 120 CrossRef PubMed
    • (2007) BMC Evol. Biol. , vol.7 , pp. 120
    • Liongue, C.1    Ward, A.C.2
  • 4
    • 0028097219 scopus 로고
    • Interaction of the growth hormone receptor cytoplasmic domain with the JAK2 tyrosine kinase
    • PubMed
    • Frank, S.J., Gilliland, G., Kraft, A.S. and Arnold, C.S. (1994) Interaction of the growth hormone receptor cytoplasmic domain with the JAK2 tyrosine kinase. Endocrinology 135, 2228-2239 PubMed
    • (1994) Endocrinology , vol.135 , pp. 2228-2239
    • Frank, S.J.1    Gilliland, G.2    Kraft, A.S.3    Arnold, C.S.4
  • 5
    • 0028956974 scopus 로고
    • Proline-rich sequence-mediated Jak2 association to the prolactin receptor is required but not sufficient for signal transduction
    • CrossRef PubMed
    • Lebrun, J.J., Ali, S., Ullrich, A. and Kelly, P.A. (1995) Proline-rich sequence-mediated Jak2 association to the prolactin receptor is required but not sufficient for signal transduction. J. Biol. Chem. 270, 10664-10670 CrossRef PubMed
    • (1995) J. Biol. Chem. , vol.270 , pp. 10664-10670
    • Lebrun, J.J.1    Ali, S.2    Ullrich, A.3    Kelly, P.A.4
  • 7
    • 0029997472 scopus 로고    scopus 로고
    • Multiple cis-trans conformers of the prolactin receptor proline-rich motif (PRM) peptide detected by reverse-phase HPLC, CD and NMR spectroscopy
    • PubMed
    • O'Neal, K.D., Chari, M. V, Mcdonald, C.H., Cook, R.G., Yu-Lee, L.Y., Morrisett, J.D. and Shearer, W.T. (1996) Multiple cis-trans conformers of the prolactin receptor proline-rich motif (PRM) peptide detected by reverse-phase HPLC, CD and NMR spectroscopy. Biochem. J. 315, 833-844 PubMed
    • (1996) Biochem. J. , vol.315 , pp. 833-844
    • O'Neal, K.D.1    Chari, M.V.2    Mcdonald, C.H.3    Cook, R.G.4    Yu-Lee, L.Y.5    Morrisett, J.D.6    Shearer, W.T.7
  • 8
    • 84879571034 scopus 로고    scopus 로고
    • β TrCP interacts with the ubiquitin-dependent endocytosis motif of the GH receptor in an unconventional manner
    • CrossRef PubMed
    • Da Silva Almeida, A.C., Hocking, H.G., Boelens, R., Strous, G.J. and van Rossum, A.G.S.H. (2013) β TrCP interacts with the ubiquitin-dependent endocytosis motif of the GH receptor in an unconventional manner. Biochem. J. 453, 291-301 CrossRef PubMed
    • (2013) Biochem. J. , vol.453 , pp. 291-301
    • Da Silva Almeida, A.C.1    Hocking, H.G.2    Boelens, R.3    Strous, G.J.4    Van Rossum, A.G.S.H.5
  • 9
    • 79960371484 scopus 로고    scopus 로고
    • Differential occurrence of protein intrinsic disorder in the cytoplasmic signaling domains of cell receptors
    • CrossRef PubMed
    • Sigalov, A.B. and Uversky, V.N. (2011) Differential occurrence of protein intrinsic disorder in the cytoplasmic signaling domains of cell receptors. Self Nonself 2, 55-72 CrossRef PubMed
    • (2011) Self Nonself , vol.2 , pp. 55-72
    • Sigalov, A.B.1    Uversky, V.N.2
  • 10
    • 50249158577 scopus 로고    scopus 로고
    • Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex
    • CrossRef PubMed
    • Skiniotis, G., Lupardus, P.J., Martick, M., Walz, T. and Garcia, K.C. (2008) Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex. Mol. Cell 31, 737-748 CrossRef PubMed
    • (2008) Mol. Cell , vol.31 , pp. 737-748
    • Skiniotis, G.1    Lupardus, P.J.2    Martick, M.3    Walz, T.4    Garcia, K.C.5
  • 11
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • CrossRef PubMed
    • Uversky, V.N. (2002) What does it mean to be natively unfolded? Eur. J. Biochem. 269, 2-12 CrossRef PubMed
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 12
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • PubMed
    • Mittag, T., Kay, L.E. and Forman-Kay, J.D. (2010) Protein dynamics and conformational disorder in molecular recognition. J. Mol. Recognit. 23, 105-116 PubMed
    • (2010) J. Mol. Recognit. , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 13
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • CrossRef PubMed
    • Oldfield, C.J., Cheng, Y., Cortese, M.S., Romero, P., Uversky, V.N. and Dunker, A.K. (2005) Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 44, 12454-12470 CrossRef PubMed
    • (2005) Biochemistry , vol.44 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 14
    • 33751526473 scopus 로고    scopus 로고
    • Ligand-independent dimerization of the human prolactin receptor isoforms: Functional implications
    • CrossRef PubMed
    • Gadd, S.L. and Clevenger, C. V (2006) Ligand-independent dimerization of the human prolactin receptor isoforms: functional implications. Mol. Endocrinol. 20, 2734-2746 CrossRef PubMed
    • (2006) Mol. Endocrinol. , vol.20 , pp. 2734-2746
    • Gadd, S.L.1    Clevenger, C.V.2
  • 18
    • 0034657348 scopus 로고    scopus 로고
    • The role of STAT proteins in growth hormone signaling
    • CrossRef PubMed
    • Herrington, J., Smit, L.S., Schwartz, J. and Carter-Su, C. (2000) The role of STAT proteins in growth hormone signaling. Oncogene 19, 2585-2597 CrossRef PubMed
    • (2000) Oncogene , vol.19 , pp. 2585-2597
    • Herrington, J.1    Smit, L.S.2    Schwartz, J.3    Carter-Su, C.4
  • 22
    • 15644367095 scopus 로고    scopus 로고
    • Growth hormone and prolactin stimulate tyrosine phosphorylation of insulin receptor substrate-1, -2, and -3, their association with p85 phosphatidylinositol 3-kinase (PI3-kinase), and concomitantly PI3-kinase activation via JAK2 kinase
    • CrossRef PubMed
    • Yamauchi, T., Yasushi, K., Ueki, K., Tsuji, Y., Stark, G.R., Kerr, I.M., Tsushima, T., Akanuma, Y., Komuro, I., Tobe, K. et al. (1998) Growth hormone and prolactin stimulate tyrosine phosphorylation of insulin receptor substrate-1, -2, and -3, their association with p85 phosphatidylinositol 3-kinase (PI3-kinase), and concomitantly PI3-kinase activation via JAK2 kinase. J. Biol. Chem. 273, 15719-15726 CrossRef PubMed
    • (1998) J. Biol. Chem. , vol.273 , pp. 15719-15726
    • Yamauchi, T.1    Yasushi, K.2    Ueki, K.3    Tsuji, Y.4    Stark, G.R.5    Kerr, I.M.6    Tsushima, T.7    Akanuma, Y.8    Komuro, I.9    Tobe, K.10
  • 23
    • 0028243306 scopus 로고
    • The protein tyrosine kinase P59fyn is associated with prolactin (PRL) receptor and is activated by PRL stimulation of T-lymphocytes
    • PubMed
    • Clevenger, C.V. and Medaglia, M.V. (1994) The protein tyrosine kinase P59fyn is associated with prolactin (PRL) receptor and is activated by PRL stimulation of T-lymphocytes. Mol. Endocrinol. 8, 674-681 PubMed
    • (1994) Mol. Endocrinol. , vol.8 , pp. 674-681
    • Clevenger, C.V.1    Medaglia, M.V.2
  • 24
    • 55449138409 scopus 로고    scopus 로고
    • Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif
    • CrossRef PubMed
    • Xu, C., Gagnon, E., Call, M.E., Schnell, J.R., Schwieters, C.D., Carman, C. V, Chou, J.J. and Wucherpfennig, K.W. (2008) Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif. Cell 135, 702-713 CrossRef PubMed
    • (2008) Cell , vol.135 , pp. 702-713
    • Xu, C.1    Gagnon, E.2    Call, M.E.3    Schnell, J.R.4    Schwieters, C.D.5    Carman, C.V.6    Chou, J.J.7    Wucherpfennig, K.W.8
  • 25
    • 0033762433 scopus 로고    scopus 로고
    • Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition
    • CrossRef PubMed
    • Aivazian, D. and Stern, L.J. (2000) Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition. Nat. Struct. Biol. 7, 1023-1026 CrossRef PubMed
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1023-1026
    • Aivazian, D.1    Stern, L.J.2
  • 26
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • CrossRef
    • Kay, L., Keifer, P. and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665 CrossRef
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.1    Keifer, P.2    Saarinen, T.3
  • 27
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • CrossRef
    • Wittekind, M. and Mueller, L. (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J. Magn. Reson. Ser. B 101, 201-205 CrossRef
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 28
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • CrossRef
    • Grzesiek, S. and Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114, 6291-6293 CrossRef
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 29
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • Kay, L.E., Ikura, M., Tschudin, R. and Bax, A. (1990) Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89, 496-514
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 30
    • 0002848358 scopus 로고
    • A constant-time three-dimensional triple-resonance pulse scheme to correlate intraresidue 1HN, 15N, and 13C' chemical shifts in 15N - 13C-labelled proteins
    • Clubb, R.T., Thanabal, V. and Wagner, G. (1992) A constant-time three-dimensional triple-resonance pulse scheme to correlate intraresidue 1HN, 15N, and 13C' chemical shifts in 15N - 13C-labelled proteins. J. Magn. Reson. 97, 213-217
    • (1992) J. Magn. Reson. , vol.97 , pp. 213-217
    • Clubb, R.T.1    Thanabal, V.2    Wagner, G.3
  • 31
    • 0034919873 scopus 로고    scopus 로고
    • Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: Application to unfolded proteins
    • CrossRef PubMed
    • Panchal, S.C., Bhavesh, N.S. and Hosur, R. V (2001) Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: application to unfolded proteins. J. Biomol. NMR 20, 135-147 CrossRef PubMed
    • (2001) J. Biomol. NMR , vol.20 , pp. 135-147
    • Panchal, S.C.1    Bhavesh, N.S.2    Hosur, R.V.3
  • 32
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • CrossRef PubMed
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 CrossRef PubMed
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 34
    • 33749524593 scopus 로고    scopus 로고
    • Automated protein structure determination from NMR spectra
    • CrossRef PubMed
    • López-Méndez, B. and G ?untert, P. (2006) Automated protein structure determination from NMR spectra. J. Am. Chem. Soc. 128, 13112-13122 CrossRef PubMed
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13112-13122
    • López-Méndez, B.1    Gúntert, P.2
  • 35
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: A database of uniformly referenced protein chemical shifts
    • CrossRef PubMed
    • Zhang, H., Neal, S. and Wishart, D.S. (2003) RefDB: a database of uniformly referenced protein chemical shifts. J. Biomol. NMR 25, 173-195 CrossRef PubMed
    • (2003) J. Biomol. NMR , vol.25 , pp. 173-195
    • Zhang, H.1    Neal, S.2    Wishart, D.S.3
  • 36
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins
    • CrossRef PubMed
    • Mulder, F. A, Schipper, D., Bott, R. and Boelens, R. (1999) Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins. J. Mol. Biol. 292, 111-123 CrossRef PubMed
    • (1999) J. Mol. Biol. , vol.292 , pp. 111-123
    • Mulder, F.A.1    Schipper, D.2    Bott, R.3    Boelens, R.4
  • 39
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • CrossRef PubMed
    • Dyson, H.J. and Wright, P.E. (2004) Unfolded proteins and protein folding studied by NMR. Chem. Rev. 104, 3607-3622 CrossRef PubMed
    • (2004) Chem. Rev. , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 40
    • 22244449320 scopus 로고    scopus 로고
    • An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family
    • CrossRef PubMed
    • McLaughlin, S., Smith, S.O., Hayman, M.J. and Murray, D. (2005) An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family. J. Gen. Physiol. 126, 41-53 CrossRef PubMed
    • (2005) J. Gen. Physiol. , vol.126 , pp. 41-53
    • McLaughlin, S.1    Smith, S.O.2    Hayman, M.J.3    Murray, D.4
  • 43
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit
    • CrossRef PubMed
    • Ehlers, M.D., Zhang, S., Bernhadt, J.P. and Huganir, R.L. (1996) Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell 84, 745-755 CrossRef PubMed
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhadt, J.P.3    Huganir, R.L.4
  • 44
    • 0037162413 scopus 로고    scopus 로고
    • The membrane-dipped neuronal SNARE complex: A site-directed spin labeling electron paramagnetic resonance study
    • CrossRef PubMed
    • Kweon, D.-H., Kim, C.S. and Shin, Y.-K. (2002) The membrane-dipped neuronal SNARE complex: a site-directed spin labeling electron paramagnetic resonance study. Biochemistry 41, 9264-9268 CrossRef PubMed
    • (2002) Biochemistry , vol.41 , pp. 9264-9268
    • Kweon, D.-H.1    Kim, C.S.2    Shin, Y.-K.3
  • 45
    • 55449093482 scopus 로고    scopus 로고
    • The safety on the TCR trigger
    • CrossRef PubMed
    • Kuhns, M.S. and Davis, M.M. (2008) The safety on the TCR trigger. Cell 135, 594-596 CrossRef PubMed
    • (2008) Cell , vol.135 , pp. 594-596
    • Kuhns, M.S.1    Davis, M.M.2
  • 46
    • 0027179487 scopus 로고
    • Phospholipids in animal eukaryotic membranes: Transverse asymmetry and movement
    • PubMed
    • Zachowski, A. (1993) Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement. Biochem. J. 294, 1-14 PubMed
    • (1993) Biochem. J. , vol.294 , pp. 1-14
    • Zachowski, A.1
  • 47
    • 70349311250 scopus 로고    scopus 로고
    • Membrane binding mode of intrinsically disordered cytoplasmic domains of T cell receptor signaling subunits depends on lipid composition
    • CrossRef PubMed
    • Sigalov, A.B. and Hendricks, G.M. (2009) Membrane binding mode of intrinsically disordered cytoplasmic domains of T cell receptor signaling subunits depends on lipid composition. Biochem. Biophys. Res. Commun. 389, 388-393 CrossRef PubMed
    • (2009) Biochem. Biophys. Res. Commun. , vol.389 , pp. 388-393
    • Sigalov, A.B.1    Hendricks, G.M.2
  • 48
    • 0036151027 scopus 로고    scopus 로고
    • ITAMs versus ITIMs: Striking a balance during cell regulation
    • CrossRef PubMed
    • Billadeau, D.D. and Leibson, P.J. (2002) ITAMs versus ITIMs: striking a balance during cell regulation. J. Clin. Invest. 109, 161-168 CrossRef PubMed
    • (2002) J. Clin. Invest. , vol.109 , pp. 161-168
    • Billadeau, D.D.1    Leibson, P.J.2
  • 49
    • 82755165363 scopus 로고    scopus 로고
    • Basic residues in the T-cell receptor ζ cytoplasmic domain mediate membrane association and modulate signaling
    • CrossRef PubMed
    • Zhang, H., Cordoba, S.-P., Dushek, O. and van der Merwe, P.A. (2011) Basic residues in the T-cell receptor ζ cytoplasmic domain mediate membrane association and modulate signaling. Proc. Natl. Acad. Sci. U.S.A. 108, 19323-19328 CrossRef PubMed
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 19323-19328
    • Zhang, H.1    Cordoba, S.-P.2    Dushek, O.3    Van Der Merwe, P.A.4
  • 50
    • 33845925345 scopus 로고    scopus 로고
    • Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits
    • CrossRef PubMed
    • Sigalov, A.B., Aivazian, D. A., Uversky, V.N. and Stern, L.J. (2006) Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits. Biochemistry 45, 15731-15739 CrossRef PubMed
    • (2006) Biochemistry , vol.45 , pp. 15731-15739
    • Sigalov, A.B.1    Aivazian, D.A.2    Uversky, V.N.3    Stern, L.J.4
  • 51
    • 0035172222 scopus 로고    scopus 로고
    • Src family kinases are required for prolactin induction of cell proliferation
    • CrossRef PubMed
    • Fresno Vara, J.A., Cáceres, M.A., Silva, A. and Martín-Pérez, J. (2001) Src family kinases are required for prolactin induction of cell proliferation. Mol. Biol. Cell 12, 2171-2183 CrossRef PubMed
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2171-2183
    • Fresno Vara, J.A.1    Cáceres, M.A.2    Silva, A.3    Martín-Pérez, J.4
  • 52
    • 0030830179 scopus 로고    scopus 로고
    • Tyrosine docking sites of the rat prolactin receptor required for association and activation of stat5
    • CrossRef PubMed
    • Pezet, A., Ferrag, F., Kelly, P.A. and Edery, M. (1997) Tyrosine docking sites of the rat prolactin receptor required for association and activation of stat5. J. Biol. Chem. 272, 25043-25050 CrossRef PubMed
    • (1997) J. Biol. Chem. , vol.272 , pp. 25043-25050
    • Pezet, A.1    Ferrag, F.2    Kelly, P.A.3    Edery, M.4
  • 53
    • 84902009569 scopus 로고    scopus 로고
    • Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
    • CrossRef PubMed
    • Wallweber, H.J.A., Tam, C., Franke, Y., Starovasnik, M.A. and Lupardus, P.J. (2014) Structural basis of recognition of interferon-α receptor by tyrosine kinase 2. Nat. Struct. Mol. Biol. 21, 443-448 CrossRef PubMed
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 443-448
    • Wallweber, H.J.A.1    Tam, C.2    Franke, Y.3    Starovasnik, M.A.4    Lupardus, P.J.5
  • 54
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • CrossRef PubMed
    • Hamada, K., Shimizu, T., Matsui, T., Tsukita, S. and Hakoshima, T. (2000) Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19, 4449-4462 CrossRef PubMed
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 55
    • 0038159324 scopus 로고    scopus 로고
    • Membrane targeting of protein tyrosine phosphatase PTPL1 through its FERM domain via binding to phosphatidylinositol 4,5-biphosphate
    • CrossRef PubMed
    • Bompard, G., Martin, M., Roy, C., Vignon, F. and Freiss, G. (2003) Membrane targeting of protein tyrosine phosphatase PTPL1 through its FERM domain via binding to phosphatidylinositol 4,5-biphosphate. J. Cell Sci. 116, 2519-2530 CrossRef PubMed
    • (2003) J. Cell Sci. , vol.116 , pp. 2519-2530
    • Bompard, G.1    Martin, M.2    Roy, C.3    Vignon, F.4    Freiss, G.5
  • 57
    • 0033521670 scopus 로고    scopus 로고
    • Identification of a novel ubiquitin conjugation motif, required for ligand-induced internalization of the growth hormone receptor
    • CrossRef PubMed
    • Govers, R., ten Broeke, T., van Kerkhof, P., Schwartz, A. L. and Strous, G.J. (1999) Identification of a novel ubiquitin conjugation motif, required for ligand-induced internalization of the growth hormone receptor. EMBO J. 18, 28-36 CrossRef PubMed
    • (1999) EMBO J. , vol.18 , pp. 28-36
    • Govers, R.1    Ten Broeke, T.2    Van Kerkhof, P.3    Schwartz, A.L.4    Strous, G.J.5
  • 58
    • 0036843906 scopus 로고    scopus 로고
    • Multiple internalization motifs differentially used by prolactin receptor isoforms mediate similar endocytic pathways
    • CrossRef PubMed
    • Lu, J.-C., Scott, P., Strous, G.J. and Schuler, L. A. (2002) Multiple internalization motifs differentially used by prolactin receptor isoforms mediate similar endocytic pathways. Mol. Endocrinol. 16, 2515-2527 CrossRef PubMed
    • (2002) Mol. Endocrinol. , vol.16 , pp. 2515-2527
    • Lu, J.-C.1    Scott, P.2    Strous, G.J.3    Schuler, L.A.4
  • 59
    • 1942453784 scopus 로고    scopus 로고
    • Negative regulation of prolactin receptor stability and signaling mediated by SCF(beta-TrCP) E3 ubiquitin ligase
    • CrossRef PubMed
    • Li, Y., Kumar, K.G.K., Tang, W., Spiegelman, V.S. and Fuchs, S.Y. (2004) Negative regulation of prolactin receptor stability and signaling mediated by SCF(beta-TrCP) E3 ubiquitin ligase. Mol. Cell. Biol. 24, 4038-4048 CrossRef PubMed
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4038-4048
    • Li, Y.1    Kumar, K.G.K.2    Tang, W.3    Spiegelman, V.S.4    Fuchs, S.Y.5
  • 60
    • 40449130327 scopus 로고    scopus 로고
    • Oncogene-mediated inhibition of glycogen synthase kinase 3 beta impairs degradation of prolactin receptor
    • CrossRef PubMed
    • Plotnikov, A., Li, Y., Tran, T.H., Tang, W., Palazzo, J.P., Rui, H. and Fuchs, S.Y. (2008) Oncogene-mediated inhibition of glycogen synthase kinase 3 beta impairs degradation of prolactin receptor. Cancer Res. 68, 1354-1361 CrossRef PubMed
    • (2008) Cancer Res. , vol.68 , pp. 1354-1361
    • Plotnikov, A.1    Li, Y.2    Tran, T.H.3    Tang, W.4    Palazzo, J.P.5    Rui, H.6    Fuchs, S.Y.7
  • 61
  • 62
    • 77956621729 scopus 로고    scopus 로고
    • Myristoylation and membrane binding regulate c-Src stability and kinase activity
    • CrossRef PubMed
    • Patwardhan, P. and Resh, M.D. (2010) Myristoylation and membrane binding regulate c-Src stability and kinase activity. Mol. Cell. Biol. 30, 4094-4107 CrossRef PubMed
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4094-4107
    • Patwardhan, P.1    Resh, M.D.2
  • 63
    • 33645818545 scopus 로고    scopus 로고
    • Plasma membrane localization of Ras requires class C Vps proteins and functional mitochondria in Saccharomyces cerevisiae
    • CrossRef PubMed
    • Wang, G. and Deschenes, R.J. (2006) Plasma membrane localization of Ras requires class C Vps proteins and functional mitochondria in Saccharomyces cerevisiae. Mol. Cell. Biol. 26, 3243-3255 CrossRef PubMed
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3243-3255
    • Wang, G.1    Deschenes, R.J.2
  • 64
    • 70249122432 scopus 로고    scopus 로고
    • The cytoplasmic tail of the T cell receptor CD3 epsilon subunit contains a phospholipid-binding motif that regulates T cell functions
    • CrossRef PubMed
    • Deford-Watts, L.M., Tassin, T.C., Becker, A.M., Medeiros, J.J., Albanesi, J.P., Love, P.E., W ?ulfing, C. and van Oers, N.S.C. (2009) The cytoplasmic tail of the T cell receptor CD3 epsilon subunit contains a phospholipid-binding motif that regulates T cell functions. J. Immunol. 183, 1055-1064 CrossRef PubMed
    • (2009) J. Immunol. , vol.183 , pp. 1055-1064
    • Deford-Watts, L.M.1    Tassin, T.C.2    Becker, A.M.3    Medeiros, J.J.4    Albanesi, J.P.5    Love, P.E.6    Wúlfing, C.7    Van Oers, N.S.C.8
  • 65
    • 33646381647 scopus 로고    scopus 로고
    • Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains
    • CrossRef PubMed
    • Lu, X., Gross, A.W. and Lodish, H.F. (2006) Active conformation of the erythropoietin receptor: random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains. J. Biol. Chem. 281, 7002-7011 CrossRef PubMed
    • (2006) J. Biol. Chem. , vol.281 , pp. 7002-7011
    • Lu, X.1    Gross, A.W.2    Lodish, H.F.3
  • 66
    • 34748853168 scopus 로고    scopus 로고
    • 13C- 13C NOESY spectra of a 480 kDa protein: Solution NMR of ferritin
    • CrossRef PubMed
    • Matzapetakis, M., Turano, P., Theil, E.C. and Bertini, I. (2007) 13C- 13C NOESY spectra of a 480 kDa protein: solution NMR of ferritin. J. Biomol. NMR 38, 237-242 CrossRef PubMed
    • (2007) J. Biomol. NMR , vol.38 , pp. 237-242
    • Matzapetakis, M.1    Turano, P.2    Theil, E.C.3    Bertini, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.