메뉴 건너뛰기




Volumn 469, Issue 3, 2016, Pages 501-506

Snapin interacts with G-protein coupled receptor PKR2

Author keywords

G protein coupled receptor; PKR2; Snapin; Yeast two hybrid

Indexed keywords

AROMATIC AMINO ACID; BINDING PROTEIN; G PROTEIN COUPLED RECEPTOR; GLUTATHIONE TRANSFERASE; PROKINETICIN RECEPTOR 2; SNAPIN; UNCLASSIFIED DRUG; PROKR2 PROTEIN, HUMAN; PROTEIN BINDING; RECEPTOR; SNAPIN PROTEIN, HUMAN; VESICULAR TRANSPORT PROTEIN;

EID: 84953455394     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.12.023     Document Type: Article
Times cited : (7)

References (38)
  • 1
    • 0035064732 scopus 로고    scopus 로고
    • Identification of two prokineticin cDNAs: Recombinant proteins potently contract gastrointestinal smooth muscle
    • M. Li, C.M. Bullock, D.J. Knauer, F.J. Ehlert, and Q.Y. Zhou Identification of two prokineticin cDNAs: recombinant proteins potently contract gastrointestinal smooth muscle Mol. Pharmacol. 59 2001 692 698
    • (2001) Mol. Pharmacol. , vol.59 , pp. 692-698
    • Li, M.1    Bullock, C.M.2    Knauer, D.J.3    Ehlert, F.J.4    Zhou, Q.Y.5
  • 2
    • 21344438597 scopus 로고    scopus 로고
    • Dependence of olfactory bulb neurogenesis on prokineticin 2 signaling
    • K.L. Ng, J.D. Li, M.Y. Cheng, F.M. Leslie, A.G. Lee, and Q.Y. Zhou Dependence of olfactory bulb neurogenesis on prokineticin 2 signaling Science 308 2005 1923 1927
    • (2005) Science , vol.308 , pp. 1923-1927
    • Ng, K.L.1    Li, J.D.2    Cheng, M.Y.3    Leslie, F.M.4    Lee, A.G.5    Zhou, Q.Y.6
  • 3
    • 84883829845 scopus 로고    scopus 로고
    • Functional analysis of the distal region of the third intracellular loop of PROKR2
    • X.T. Zhou, D.N. Chen, Z.Q. Xie, and et al. Functional analysis of the distal region of the third intracellular loop of PROKR2 Biochem. Biophys. Res. Commun. 439 2013 12 17
    • (2013) Biochem. Biophys. Res. Commun. , vol.439 , pp. 12-17
    • Zhou, X.T.1    Chen, D.N.2    Xie, Z.Q.3
  • 4
    • 79955753988 scopus 로고    scopus 로고
    • Disease-causing mutation in PKR2 receptor reveals a critical role of positive charges in the second intracellular loop for G-protein coupling and receptor trafficking
    • Z. Peng, Y. Tang, H. Luo, and et al. Disease-causing mutation in PKR2 receptor reveals a critical role of positive charges in the second intracellular loop for G-protein coupling and receptor trafficking J. Biol. Chem. 286 2011 16615 16622
    • (2011) J. Biol. Chem. , vol.286 , pp. 16615-16622
    • Peng, Z.1    Tang, Y.2    Luo, H.3
  • 5
    • 41149095020 scopus 로고    scopus 로고
    • Mitogenic functions of endocrine gland-derived vascular endothelial growth factor and Bombina variegata 8 on steroidogenic adrenocortical cells
    • M. Keramidas, C. Faudot, A. Cibiel, J.J. Feige, and M. Thomas Mitogenic functions of endocrine gland-derived vascular endothelial growth factor and Bombina variegata 8 on steroidogenic adrenocortical cells J. Endocrinol. 196 2008 473 482
    • (2008) J. Endocrinol. , vol.196 , pp. 473-482
    • Keramidas, M.1    Faudot, C.2    Cibiel, A.3    Feige, J.J.4    Thomas, M.5
  • 6
    • 33645219817 scopus 로고    scopus 로고
    • Abnormal development of the olfactory bulb and reproductive system in mice lacking prokineticin receptor PKR2
    • S. Matsumoto, C. Yamazaki, K.H. Masumoto, and et al. Abnormal development of the olfactory bulb and reproductive system in mice lacking prokineticin receptor PKR2 Proc. Natl. Acad. Sci. U. S. A. 103 2006 4140 4145
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4140-4145
    • Matsumoto, S.1    Yamazaki, C.2    Masumoto, K.H.3
  • 7
    • 36849044530 scopus 로고    scopus 로고
    • Loss-of-function mutation in the prokineticin 2 gene causes Kallmann syndrome and normosmic idiopathic hypogonadotropic hypogonadism
    • N. Pitteloud, C. Zhang, D. Pignatelli, and et al. Loss-of-function mutation in the prokineticin 2 gene causes Kallmann syndrome and normosmic idiopathic hypogonadotropic hypogonadism Proc. Natl. Acad. Sci. U. S. A. 104 2007 17447 17452
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 17447-17452
    • Pitteloud, N.1    Zhang, C.2    Pignatelli, D.3
  • 8
    • 85047688237 scopus 로고    scopus 로고
    • Functional rescue of Kallmann syndrome- associated prokineticin receptor 2 (PKR2) mutants deficient in trafficking
    • D.N. Chen, Y.T. Ma, H. Liu, Q.Y. Zhou, and J.D. Li Functional rescue of Kallmann syndrome- associated prokineticin receptor 2 (PKR2) mutants deficient in trafficking J. Biol. Chem. 289 2014 15518 15526
    • (2014) J. Biol. Chem. , vol.289 , pp. 15518-15526
    • Chen, D.N.1    Ma, Y.T.2    Liu, H.3    Zhou, Q.Y.4    Li, J.D.5
  • 9
    • 33751107191 scopus 로고    scopus 로고
    • Attenuated circadian rhythms in mice lacking the prokineticin 2 gene
    • J.D. Li, W.P. Hu, L. Boehmer, and et al. Attenuated circadian rhythms in mice lacking the prokineticin 2 gene J. Neurosci. 26 2006 11615 11623
    • (2006) J. Neurosci. , vol.26 , pp. 11615-11623
    • Li, J.D.1    Hu, W.P.2    Boehmer, L.3
  • 10
    • 0034862452 scopus 로고    scopus 로고
    • Beta-Arrestins: New roles in regulating heptahelical receptors' functions
    • P.H. McDonald, and R.J. Lefkowitz Beta-Arrestins: new roles in regulating heptahelical receptors' functions Cell Signal. 13 2001 683 689
    • (2001) Cell Signal. , vol.13 , pp. 683-689
    • McDonald, P.H.1    Lefkowitz, R.J.2
  • 12
    • 0242721361 scopus 로고    scopus 로고
    • Multifaceted roles of beta-arrestins in the regulation of seven- membrane-spanning receptor trafficking and signalling
    • S.K. Shenoy, and R.J. Lefkowitz Multifaceted roles of beta-arrestins in the regulation of seven- membrane-spanning receptor trafficking and signalling Biochem. J. 375 2003 503 515
    • (2003) Biochem. J. , vol.375 , pp. 503-515
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 13
    • 0037737763 scopus 로고    scopus 로고
    • Trafficking patterns of beta-arrestin and G protein-coupled receptors determined by the kinetics of beta-arrestin deubiquitination
    • S.K. Shenoy, and R.J. Lefkowitz Trafficking patterns of beta-arrestin and G protein-coupled receptors determined by the kinetics of beta-arrestin deubiquitination J. Biol. Chem. 278 2003 14498 14506
    • (2003) J. Biol. Chem. , vol.278 , pp. 14498-14506
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 14
    • 0037205491 scopus 로고    scopus 로고
    • Identification and molecular characterization of two closely related G protein-coupled receptors activated by prokineticins/endocrine gland vascular endothelial growth factor
    • D.C. Lin, C.M. Bullock, F.J. Ehlert, J.L. Chen, H. Tian, and Q.Y. Zhou Identification and molecular characterization of two closely related G protein-coupled receptors activated by prokineticins/endocrine gland vascular endothelial growth factor J. Biol. Chem. 277 2002 19276 19280
    • (2002) J. Biol. Chem. , vol.277 , pp. 19276-19280
    • Lin, D.C.1    Bullock, C.M.2    Ehlert, F.J.3    Chen, J.L.4    Tian, H.5    Zhou, Q.Y.6
  • 15
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • J.M. Ilardi, S. Mochida, and Z.H. Sheng Snapin: a SNARE-associated protein implicated in synaptic transmission Nat. Neurosci. 2 1999 119 124
    • (1999) Nat. Neurosci. , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.H.3
  • 16
    • 0142138839 scopus 로고    scopus 로고
    • Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells
    • P. Buxton, X.M. Zhang, B. Walsh, and et al. Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells Biochem. J. 375 2003 433 440
    • (2003) Biochem. J. , vol.375 , pp. 433-440
    • Buxton, P.1    Zhang, X.M.2    Walsh, B.3
  • 17
    • 33745480157 scopus 로고    scopus 로고
    • Ryanodine receptor interaction with the SNARE-associated protein snapin
    • S. Zissimopoulos, D.J. West, A.J. Williams, and F.A. Lai Ryanodine receptor interaction with the SNARE-associated protein snapin J. Cell Sci. 119 2006 2386 2397
    • (2006) J. Cell Sci. , vol.119 , pp. 2386-2397
    • Zissimopoulos, S.1    West, D.J.2    Williams, A.J.3    Lai, F.A.4
  • 18
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ- domain interaction controls endocytic sorting of the beta2-adrenergic receptor
    • T.T. Cao, H.W. Deacon, D. Reczek, A. Bretscher, and M. von Zastrow A kinase-regulated PDZ- domain interaction controls endocytic sorting of the beta2-adrenergic receptor Nature 401 1999 286 290
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3    Bretscher, A.4    Von Zastrow, M.5
  • 19
    • 0035977051 scopus 로고    scopus 로고
    • Binding of the beta2 adrenergic receptor to N-ethylmaleimide-sensitive factor regulates receptor recycling
    • M. Cong, S.J. Perry, L.A. Hu, P.I. Hanson, A. Claing, and R.J. Lefkowitz Binding of the beta2 adrenergic receptor to N-ethylmaleimide-sensitive factor regulates receptor recycling J. Biol. Chem. 276 2001 45145 45152
    • (2001) J. Biol. Chem. , vol.276 , pp. 45145-45152
    • Cong, M.1    Perry, S.J.2    Hu, L.A.3    Hanson, P.I.4    Claing, A.5    Lefkowitz, R.J.6
  • 20
    • 11144229682 scopus 로고    scopus 로고
    • A library of 7TM receptor C-terminal tails. Interactions with the proposed post-endocytic sorting proteins ERM-binding phosphoprotein 50 (EBP50), N-ethylmaleimide-sensitive factor (NSF), sorting nexin 1 (SNX1), and G protein-coupled receptor-associated sorting protein (GASP)
    • A. Heydorn, B.P. Sondergaard, B. Ersboll, and et al. A library of 7TM receptor C-terminal tails. Interactions with the proposed post-endocytic sorting proteins ERM-binding phosphoprotein 50 (EBP50), N-ethylmaleimide-sensitive factor (NSF), sorting nexin 1 (SNX1), and G protein-coupled receptor-associated sorting protein (GASP) J. Biol. Chem. 279 2004 54291 54303
    • (2004) J. Biol. Chem. , vol.279 , pp. 54291-54303
    • Heydorn, A.1    Sondergaard, B.P.2    Ersboll, B.3
  • 21
    • 13544253361 scopus 로고    scopus 로고
    • Type I PDZ ligands are sufficient to promote rapid recycling of G Protein-coupled receptors independent of binding to N-ethylmaleimide-sensitive factor
    • R.M. Gage, E.A. Matveeva, S.W. Whiteheart, and M. von Zastrow Type I PDZ ligands are sufficient to promote rapid recycling of G Protein-coupled receptors independent of binding to N-ethylmaleimide-sensitive factor J. Biol. Chem. 280 2005 3305 3313
    • (2005) J. Biol. Chem. , vol.280 , pp. 3305-3313
    • Gage, R.M.1    Matveeva, E.A.2    Whiteheart, S.W.3    Von Zastrow, M.4
  • 22
    • 0037178820 scopus 로고    scopus 로고
    • Ezrin-radixin-moesin-binding phosphoprotein-50/Na+/H+ exchanger regulatory factor (EBP50/NHERF) blocks U50,488H-induced down-regulation of the human kappa opioid receptor by enhancing its recycling rate
    • J.G. Li, C. Chen, and L.Y. Liu-Chen Ezrin-radixin-moesin-binding phosphoprotein-50/Na+/H+ exchanger regulatory factor (EBP50/NHERF) blocks U50,488H-induced down-regulation of the human kappa opioid receptor by enhancing its recycling rate J. Biol. Chem. 277 2002 27545 27552
    • (2002) J. Biol. Chem. , vol.277 , pp. 27545-27552
    • Li, J.G.1    Chen, C.2    Liu-Chen, L.Y.3
  • 23
    • 0037178754 scopus 로고    scopus 로고
    • Modulation of postendocytic sorting of G protein-coupled receptors
    • J.L. Whistler, J. Enquist, A. Marley, and et al. Modulation of postendocytic sorting of G protein-coupled receptors Science 297 2002 615 620
    • (2002) Science , vol.297 , pp. 615-620
    • Whistler, J.L.1    Enquist, J.2    Marley, A.3
  • 24
    • 0035985175 scopus 로고    scopus 로고
    • Down-regulation of protease-activated receptor-1 is regulated by sorting nexin 1
    • Y. Wang, Y. Zhou, K. Szabo, C.R. Haft, and J. Trejo Down-regulation of protease-activated receptor-1 is regulated by sorting nexin 1 Mol. Biol. Cell 13 2002 1965 1976
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1965-1976
    • Wang, Y.1    Zhou, Y.2    Szabo, K.3    Haft, C.R.4    Trejo, J.5
  • 25
    • 0038532256 scopus 로고    scopus 로고
    • Binding of filamin to the C-terminal tail of the calcitonin receptor controls recycling
    • T. Seck, R. Baron, and W.C. Horne Binding of filamin to the C-terminal tail of the calcitonin receptor controls recycling J. Biol. Chem. 278 2003 10408 10416
    • (2003) J. Biol. Chem. , vol.278 , pp. 10408-10416
    • Seck, T.1    Baron, R.2    Horne, W.C.3
  • 26
    • 0842292006 scopus 로고    scopus 로고
    • GIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHR
    • T. Hirakawa, C. Galet, M. Kishi, and M. Ascoli GIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHR J. Biol. Chem. 278 2003 49348 49357
    • (2003) J. Biol. Chem. , vol.278 , pp. 49348-49357
    • Hirakawa, T.1    Galet, C.2    Kishi, M.3    Ascoli, M.4
  • 27
    • 4143144446 scopus 로고    scopus 로고
    • Crucial role of neuron-enriched endosomal protein of 21 kDa in sorting between degradation and recycling of internalized G-protein-coupled receptors
    • C. Debaigt, H. Hirling, P. Steiner, J.P. Vincent, and J. Mazella Crucial role of neuron-enriched endosomal protein of 21 kDa in sorting between degradation and recycling of internalized G-protein-coupled receptors J. Biol. Chem. 279 2004 35687 35691
    • (2004) J. Biol. Chem. , vol.279 , pp. 35687-35691
    • Debaigt, C.1    Hirling, H.2    Steiner, P.3    Vincent, J.P.4    Mazella, J.5
  • 28
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: An evolutionary success
    • J. Bockaert, and J.P. Pin Molecular tinkering of G protein-coupled receptors: an evolutionary success EMBO J. 18 1999 1723 1729
    • (1999) EMBO J. , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 29
    • 77955984298 scopus 로고    scopus 로고
    • The crystallographic structure of the human adenosine A2A receptor in a high-affinity antagonist-bound state: Implications for GPCR drug screening and design
    • V.P. Jaakola, and A.P. Ijzerman The crystallographic structure of the human adenosine A2A receptor in a high-affinity antagonist-bound state: implications for GPCR drug screening and design Curr. Opin. Struct. Biol. 20 2010 401 414
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 401-414
    • Jaakola, V.P.1    Ijzerman, A.P.2
  • 30
    • 84896732724 scopus 로고    scopus 로고
    • Mechanisms that underlie the internalization and extracellular signal regulated kinase 1/2 activation by PKR2 receptor
    • W. Yin, H. Liu, Z. Peng, D. Chen, J. Li, and J.D. Li Mechanisms that underlie the internalization and extracellular signal regulated kinase 1/2 activation by PKR2 receptor Cell Signal. 26 2014 1118 1124
    • (2014) Cell Signal. , vol.26 , pp. 1118-1124
    • Yin, W.1    Liu, H.2    Peng, Z.3    Chen, D.4    Li, J.5    Li, J.D.6
  • 31
    • 0037862083 scopus 로고    scopus 로고
    • The 'magic tail' of G protein-coupled receptors: An anchorage for functional protein networks
    • J. Bockaert, P. Marin, A. Dumuis, and L. Fagni The 'magic tail' of G protein-coupled receptors: an anchorage for functional protein networks FEBS Lett. 546 2003 65 72
    • (2003) FEBS Lett. , vol.546 , pp. 65-72
    • Bockaert, J.1    Marin, P.2    Dumuis, A.3    Fagni, L.4
  • 32
    • 2342470026 scopus 로고    scopus 로고
    • Identification and functional roles of metabotropic glutamate receptor-interacting proteins
    • L. Fagni, F. Ango, J. Perroy, and J. Bockaert Identification and functional roles of metabotropic glutamate receptor-interacting proteins Semin. Cell Dev. Biol. 15 2004 289 298
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 289-298
    • Fagni, L.1    Ango, F.2    Perroy, J.3    Bockaert, J.4
  • 33
    • 0242353156 scopus 로고    scopus 로고
    • PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase, preventing neuronal apoptosis
    • R. Rong, J.Y. Ahn, H. Huang, and et al. PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase, preventing neuronal apoptosis Nat. Neurosci. 6 2003 1153 1161
    • (2003) Nat. Neurosci. , vol.6 , pp. 1153-1161
    • Rong, R.1    Ahn, J.Y.2    Huang, H.3
  • 34
    • 0034141207 scopus 로고    scopus 로고
    • Complex interactions between mGluRs, intracellular Ca2+ stores and ion channels in neurons
    • L. Fagni, P. Chavis, F. Ango, and J. Bockaert Complex interactions between mGluRs, intracellular Ca2+ stores and ion channels in neurons Trends Neurosci. 23 2000 80 88
    • (2000) Trends Neurosci. , vol.23 , pp. 80-88
    • Fagni, L.1    Chavis, P.2    Ango, F.3    Bockaert, J.4
  • 35
    • 84938747698 scopus 로고    scopus 로고
    • Regulation of synaptic activity by snapin-mediated endolysosomal transport and sorting
    • J. Di Giovanni, and Z.H. Sheng Regulation of synaptic activity by snapin-mediated endolysosomal transport and sorting EMBO J. 34 2015 2059 2077
    • (2015) EMBO J. , vol.34 , pp. 2059-2077
    • Di Giovanni, J.1    Sheng, Z.H.2
  • 36
    • 79953659794 scopus 로고    scopus 로고
    • Uncovering the role of Snapin in regulating autophagy-lysosomal function
    • Q. Cai, and Z.H. Sheng Uncovering the role of Snapin in regulating autophagy-lysosomal function Autophagy 7 2011 445 447
    • (2011) Autophagy , vol.7 , pp. 445-447
    • Cai, Q.1    Sheng, Z.H.2
  • 37
    • 84937148634 scopus 로고    scopus 로고
    • Axonal autophagosomes recruit dynein for retrograde transport through fusion with late endosomes
    • X.T. Cheng, B. Zhou, M.Y. Lin, Q. Cai, and Z.H. Sheng Axonal autophagosomes recruit dynein for retrograde transport through fusion with late endosomes J. Cell Biol. 209 2015 377 386
    • (2015) J. Cell Biol. , vol.209 , pp. 377-386
    • Cheng, X.T.1    Zhou, B.2    Lin, M.Y.3    Cai, Q.4    Sheng, Z.H.5
  • 38
    • 35748941237 scopus 로고    scopus 로고
    • Snapin, a new regulator of receptor signaling, augments alpha1A-adrenoceptor-operated calcium influx through TRPC6
    • F. Suzuki, S. Morishima, T. Tanaka, and I. Muramatsu Snapin, a new regulator of receptor signaling, augments alpha1A-adrenoceptor-operated calcium influx through TRPC6 J. Biol. Chem. 282 2007 29563 29573
    • (2007) J. Biol. Chem. , vol.282 , pp. 29563-29573
    • Suzuki, F.1    Morishima, S.2    Tanaka, T.3    Muramatsu, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.