메뉴 건너뛰기




Volumn 25, Issue 10, 2004, Pages 528-535

PKC-interacting proteins: From function to pharmacology

Author keywords

[No Author keywords available]

Indexed keywords

FASCIN; ISOENZYME; LAMIN A; PERICENTRIN; PROTEIN DERIVATIVE; PROTEIN KINASE C; PROTEIN KINASE C ALPHA; PROTEIN KINASE C BETA; PROTEIN KINASE C BETA1; PROTEIN KINASE C BETA2; PROTEIN KINASE C DELTA; PROTEIN KINASE C EPSILON; PROTEIN KINASE C GAMMA; PROTEIN KINASE C THETA; PROTEIN KINASE C ZETA; PROTEIN KINASE LCK; PROTEOME; UNCLASSIFIED DRUG; Z BAND ALTERNATIVELY SPLICED PDZ DOMAIN CONTAINING PROTEIN;

EID: 4544323559     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2004.08.006     Document Type: Review
Times cited : (121)

References (70)
  • 2
    • 0034057863 scopus 로고    scopus 로고
    • Protein kinase C binding partners
    • S. Jaken, and P.J. Parker Protein kinase C binding partners BioEssays 22 2000 245 254
    • (2000) BioEssays , vol.22 , pp. 245-254
    • Jaken, S.1    Parker, P.J.2
  • 3
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • A.C. Newton Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm Biochem. J. 370 2003 361 371
    • (2003) Biochem. J. , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 4
    • 0036196195 scopus 로고    scopus 로고
    • Intracellular transport mechanisms of signal transducers
    • G.W.n Dorn, and D. Mochly-Rosen Intracellular transport mechanisms of signal transducers Annu. Rev. Physiol. 64 2002 407 429
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 407-429
    • Dorn, G.W.N.1    Mochly-Rosen, D.2
  • 5
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • D. Mochly-Rosen Localization of protein kinases by anchoring proteins: a theme in signal transduction Science 268 1995 247 251
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 6
    • 0034328882 scopus 로고    scopus 로고
    • The atypical protein kinase Cs. Functional specificity mediated by specific protein adapters
    • J. Moscat, and M.T. Diaz-Meco The atypical protein kinase Cs. Functional specificity mediated by specific protein adapters EMBO Rep. 1 2000 399 403
    • (2000) EMBO Rep. , vol.1 , pp. 399-403
    • Moscat, J.1    Diaz-Meco, M.T.2
  • 7
    • 85047682875 scopus 로고    scopus 로고
    • Protein kinase C(theta) in T cell activation
    • N. Isakov, and A. Altman Protein kinase C(theta) in T cell activation Annu. Rev. Immunol. 20 2002 761 794
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 761-794
    • Isakov, N.1    Altman, A.2
  • 8
    • 0035474310 scopus 로고    scopus 로고
    • Adaptor proteins in protein kinase C-mediated signal transduction
    • D. Schechtman, and D. Mochly-Rosen Adaptor proteins in protein kinase C-mediated signal transduction Oncogene 20 2001 6339 6347
    • (2001) Oncogene , vol.20 , pp. 6339-6347
    • Schechtman, D.1    Mochly-Rosen, D.2
  • 9
    • 0033119158 scopus 로고    scopus 로고
    • Pharmacologic modulation of protein kinase C isozymes: The role of RACKs and subcellular localisation
    • M. Csukai, and D. Mochly-Rosen Pharmacologic modulation of protein kinase C isozymes: the role of RACKs and subcellular localisation Pharmacol. Res. 39 1999 253 259
    • (1999) Pharmacol. Res. , vol.39 , pp. 253-259
    • Csukai, M.1    Mochly-Rosen, D.2
  • 10
    • 0031761325 scopus 로고    scopus 로고
    • Peptide modulators of protein-protein interactions in intracellular signaling
    • M.C. Souroujon, and D. Mochly-Rosen Peptide modulators of protein-protein interactions in intracellular signaling Nat. Biotechnol. 16 1998 919 924
    • (1998) Nat. Biotechnol. , vol.16 , pp. 919-924
    • Souroujon, M.C.1    Mochly-Rosen, D.2
  • 11
    • 10744231114 scopus 로고    scopus 로고
    • A Cypher/ZASP mutation associated with dilated cardiomyopathy alters the binding affinity to protein kinase C
    • T. Arimura A Cypher/ZASP mutation associated with dilated cardiomyopathy alters the binding affinity to protein kinase C J. Biol. Chem. 279 2004 6746 6752
    • (2004) J. Biol. Chem. , vol.279 , pp. 6746-6752
    • Arimura, T.1
  • 12
    • 0034958672 scopus 로고    scopus 로고
    • Localization, anchoring, and functions of protein kinase C isozymes in the heart
    • K. Mackay, and D. Mochly-Rosen Localization, anchoring, and functions of protein kinase C isozymes in the heart J. Mol. Cell. Cardiol. 33 2001 1301 1307
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 1301-1307
    • MacKay, K.1    Mochly-Rosen, D.2
  • 13
    • 0034625662 scopus 로고    scopus 로고
    • Cardiotrophic effects of protein kinase C epsilon: Analysis by in vivo modulation of PKCepsilon translocation
    • D. Mochly-Rosen Cardiotrophic effects of protein kinase C epsilon: analysis by in vivo modulation of PKCepsilon translocation Circ. Res. 86 2000 1173 1179
    • (2000) Circ. Res. , vol.86 , pp. 1173-1179
    • Mochly-Rosen, D.1
  • 14
    • 0035662009 scopus 로고    scopus 로고
    • Enhanced PKC beta II translocation and PKC beta II-RACK1 interactions in PKC epsilon-induced heart failure: A role for RACK1
    • J.M. Pass Enhanced PKC beta II translocation and PKC beta II-RACK1 interactions in PKC epsilon-induced heart failure: a role for RACK1 Am. J. Physiol. Heart Circ. Physiol. 281 2001 H2500 H2510
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281
    • Pass, J.M.1
  • 15
    • 1042266629 scopus 로고    scopus 로고
    • Centrosomal anchoring of protein kinase C betaII by pericentrin controls microtubule organization, spindle function, and cytokinesis
    • D. Chen Centrosomal anchoring of protein kinase C betaII by pericentrin controls microtubule organization, spindle function, and cytokinesis J. Biol. Chem. 279 2004 4829 4839
    • (2004) J. Biol. Chem. , vol.279 , pp. 4829-4839
    • Chen, D.1
  • 16
    • 0142073731 scopus 로고    scopus 로고
    • Interaction of fascin and protein kinase Calpha: A novel intersection in cell adhesion and motility
    • N. Anilkumar Interaction of fascin and protein kinase Calpha: a novel intersection in cell adhesion and motility EMBO J. 22 2003 5390 5402
    • (2003) EMBO J. , vol.22 , pp. 5390-5402
    • Anilkumar, N.1
  • 17
    • 0345356539 scopus 로고    scopus 로고
    • Opposing roles of delta and epsilonPKC in cardiac ischemia and reperfusion: Targeting the apoptotic machinery
    • C.L. Murriel, and D. Mochly-Rosen Opposing roles of delta and epsilonPKC in cardiac ischemia and reperfusion: targeting the apoptotic machinery Arch. Biochem. Biophys. 420 2003 246 254
    • (2003) Arch. Biochem. Biophys. , vol.420 , pp. 246-254
    • Murriel, C.L.1    Mochly-Rosen, D.2
  • 18
    • 0035910607 scopus 로고    scopus 로고
    • Functional proteomic analysis of protein kinase C epsilon signaling complexes in the normal heart and during cardioprotection
    • P. Ping Functional proteomic analysis of protein kinase C epsilon signaling complexes in the normal heart and during cardioprotection Circ. Res. 88 2001 59 62
    • (2001) Circ. Res. , vol.88 , pp. 59-62
    • Ping, P.1
  • 19
    • 0036177969 scopus 로고    scopus 로고
    • Formation of protein kinase C(epsilon)-Lck signaling modules confers cardioprotection
    • P. Ping Formation of protein kinase C(epsilon)-Lck signaling modules confers cardioprotection J. Clin. Invest. 109 2002 499 507
    • (2002) J. Clin. Invest. , vol.109 , pp. 499-507
    • Ping, P.1
  • 20
    • 0037155856 scopus 로고    scopus 로고
    • Interaction of Bruton's tyrosine kinase and protein kinase Ctheta in platelets. Cross-talk between tyrosine and serine/threonine kinases
    • D. Crosby, and A.W. Poole Interaction of Bruton's tyrosine kinase and protein kinase Ctheta in platelets. Cross-talk between tyrosine and serine/threonine kinases J. Biol. Chem. 277 2002 9958 9965
    • (2002) J. Biol. Chem. , vol.277 , pp. 9958-9965
    • Crosby, D.1    Poole, A.W.2
  • 21
    • 1642535447 scopus 로고    scopus 로고
    • Differential role of protein kinase C delta isoform in agonist-induced dense granule secretion in human platelets
    • S. Murugappan Differential role of protein kinase C delta isoform in agonist-induced dense granule secretion in human platelets J. Biol. Chem. 279 2004 2360 2367
    • (2004) J. Biol. Chem. , vol.279 , pp. 2360-2367
    • Murugappan, S.1
  • 22
    • 0036258094 scopus 로고    scopus 로고
    • Protein kinase C-delta is a negative regulator of antigen-induced mast cell degranulation
    • M. Leitges Protein kinase C-delta is a negative regulator of antigen-induced mast cell degranulation Mol. Cell. Biol. 22 2002 3970 3980
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3970-3980
    • Leitges, M.1
  • 23
    • 0043092028 scopus 로고    scopus 로고
    • Physical and functional interaction between protein kinase C delta and Fyn tyrosine kinase in human platelets
    • D. Crosby, and A.W. Poole Physical and functional interaction between protein kinase C delta and Fyn tyrosine kinase in human platelets J. Biol. Chem. 278 2003 24533 24541
    • (2003) J. Biol. Chem. , vol.278 , pp. 24533-24541
    • Crosby, D.1    Poole, A.W.2
  • 24
    • 0031964645 scopus 로고    scopus 로고
    • Anchoring proteins for protein kinase C: A means for isozyme selectivity
    • D. Mochly-Rosen, and A.S. Gordon Anchoring proteins for protein kinase C: a means for isozyme selectivity FASEB J. 12 1998 35 42
    • (1998) FASEB J. , vol.12 , pp. 35-42
    • Mochly-Rosen, D.1    Gordon, A.S.2
  • 25
    • 0030965165 scopus 로고    scopus 로고
    • An inhibitory fragment derived from protein kinase Cepsilon prevents enhancement of nerve growth factor responses by ethanol and phorbol esters
    • B. Hundle An inhibitory fragment derived from protein kinase Cepsilon prevents enhancement of nerve growth factor responses by ethanol and phorbol esters J. Biol. Chem. 272 1997 15028 15035
    • (1997) J. Biol. Chem. , vol.272 , pp. 15028-15035
    • Hundle, B.1
  • 26
    • 13044274187 scopus 로고    scopus 로고
    • Sustained in vivo cardiac protection by a rationally designed peptide that causes epsilon protein kinase C translocation
    • G.W.n. Dorn Sustained in vivo cardiac protection by a rationally designed peptide that causes epsilon protein kinase C translocation Proc. Natl. Acad. Sci. U. S. A. 96 1999 12798 12803
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 12798-12803
    • Dorn, G.W.N.1
  • 27
    • 2442546710 scopus 로고    scopus 로고
    • Biodistribution of intracellularly acting peptides conjugated reversibly to Tat
    • R. Begley Biodistribution of intracellularly acting peptides conjugated reversibly to Tat Biochem. Biophys. Res. Commun. 318 2004 949 954
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 949-954
    • Begley, R.1
  • 28
    • 0041932511 scopus 로고    scopus 로고
    • Additive Protection of the Ischemic Heart ex vivo by Combined Treatment with delta-Protein Kinase C Inhibitor and epsilon Protein Kinase C Activator
    • K. Inagaki Additive Protection of the Ischemic Heart ex vivo by Combined Treatment With delta-Protein Kinase C Inhibitor and epsilon Protein Kinase C Activator Circulation 108 2003 869 875
    • (2003) Circulation , vol.108 , pp. 869-875
    • Inagaki, K.1
  • 29
    • 0035986315 scopus 로고    scopus 로고
    • Molecular characterization of protein kinase C-alpha binding to lamin a
    • A.M. Martelli Molecular characterization of protein kinase C-alpha binding to lamin A J. Cell. Biochem. 86 2002 320 330
    • (2002) J. Cell. Biochem. , vol.86 , pp. 320-330
    • Martelli, A.M.1
  • 30
    • 0346094408 scopus 로고    scopus 로고
    • Recent developments in the analysis of protein complexes
    • A. Dziembowski, and B. Seraphin Recent developments in the analysis of protein complexes FEBS Lett. 556 2004 1 6
    • (2004) FEBS Lett. , vol.556 , pp. 1-6
    • Dziembowski, A.1    Seraphin, B.2
  • 31
    • 0037451177 scopus 로고    scopus 로고
    • Association of diacylglycerol kinase zeta with protein kinase C alpha: Spatial regulation of diacylglycerol signaling
    • B. Luo Association of diacylglycerol kinase zeta with protein kinase C alpha: spatial regulation of diacylglycerol signaling J. Cell Biol. 160 2003 929 937
    • (2003) J. Cell Biol. , vol.160 , pp. 929-937
    • Luo, B.1
  • 32
    • 0038607443 scopus 로고    scopus 로고
    • The F-actin cross-linking and focal adhesion protein filamin a is a ligand and in vivo substrate for protein kinase C alpha
    • U. Tigges The F-actin cross-linking and focal adhesion protein filamin A is a ligand and in vivo substrate for protein kinase C alpha J. Biol. Chem. 278 2003 23561 23569
    • (2003) J. Biol. Chem. , vol.278 , pp. 23561-23569
    • Tigges, U.1
  • 33
    • 0035996587 scopus 로고    scopus 로고
    • Binding of elements of protein kinase C-alpha regulatory domain to lamin B1
    • G. Tabellini Binding of elements of protein kinase C-alpha regulatory domain to lamin B1 Cell. Signal. 14 2002 819 827
    • (2002) Cell. Signal. , vol.14 , pp. 819-827
    • Tabellini, G.1
  • 34
    • 2542495782 scopus 로고    scopus 로고
    • Regulation of phospholipase D2 activity by protein kinase Calpha
    • J.S. Chen, and J.H. Exton Regulation of phospholipase D2 activity by protein kinase Calpha J. Biol. Chem. 279 2004 22076 22083
    • (2004) J. Biol. Chem. , vol.279 , pp. 22076-22083
    • Chen, J.S.1    Exton, J.H.2
  • 35
    • 1642545636 scopus 로고    scopus 로고
    • Syndecan-4 regulates localization, activity and stability of protein kinase C-alpha
    • E. Keum Syndecan-4 regulates localization, activity and stability of protein kinase C-alpha Biochem. J. 378 2004 1007 1014
    • (2004) Biochem. J. , vol.378 , pp. 1007-1014
    • Keum, E.1
  • 36
    • 0037456522 scopus 로고    scopus 로고
    • Rapid and differential regulation of AMPA and kainate receptors at hippocampal mossy fibre synapses by PICK1 and GRIP
    • H. Hirbec Rapid and differential regulation of AMPA and kainate receptors at hippocampal mossy fibre synapses by PICK1 and GRIP Neuron 37 2003 625 638
    • (2003) Neuron , vol.37 , pp. 625-638
    • Hirbec, H.1
  • 37
    • 0042090412 scopus 로고    scopus 로고
    • A catalytically inactive form of protein kinase C-associated kinase/receptor interacting protein 4, a protein kinase C beta-associated kinase that mediates NF-kappa B activation, interferes with early B cell development
    • A. Cariappa A catalytically inactive form of protein kinase C-associated kinase/receptor interacting protein 4, a protein kinase C beta-associated kinase that mediates NF-kappa B activation, interferes with early B cell development J. Immunol. 171 2003 1875 1880
    • (2003) J. Immunol. , vol.171 , pp. 1875-1880
    • Cariappa, A.1
  • 38
    • 4043139440 scopus 로고    scopus 로고
    • PH domain of G protein-coupled receptor kinase-2 binds to protein kinase C (PKC) and negatively regulates activity of PKC kinase
    • S. Ji PH domain of G protein-coupled receptor kinase-2 binds to protein kinase C (PKC) and negatively regulates activity of PKC kinase Front. Biosci. 8 2003 a34 a39
    • (2003) Front. Biosci. , vol.8
    • Ji, S.1
  • 39
    • 0141532040 scopus 로고    scopus 로고
    • Differential and regulated binding of cAMP-dependent protein kinase and protein kinase C isoenzymes to gravin in human model neurons: Evidence that gravin provides a dynamic platform for the localization for kinases during neuronal development
    • J. Piontek, and R. Brandt Differential and regulated binding of cAMP-dependent protein kinase and protein kinase C isoenzymes to gravin in human model neurons: Evidence that gravin provides a dynamic platform for the localization for kinases during neuronal development J. Biol. Chem. 278 2003 38970 38979
    • (2003) J. Biol. Chem. , vol.278 , pp. 38970-38979
    • Piontek, J.1    Brandt, R.2
  • 40
    • 0242321123 scopus 로고    scopus 로고
    • Regulation of the insulin receptor by protein kinase C isoenzymes: Preferential interaction with beta isoenzymes and interaction with the catalytic domain of betaII
    • T.S. Pillay Regulation of the insulin receptor by protein kinase C isoenzymes: preferential interaction with beta isoenzymes and interaction with the catalytic domain of betaII Cell. Signal. 16 2004 97 104
    • (2004) Cell. Signal. , vol.16 , pp. 97-104
    • Pillay, T.S.1
  • 41
    • 0037303131 scopus 로고    scopus 로고
    • Stability of actin cytoskeleton and PKC-delta binding to actin regulate NKCC1 function in airway epithelial cells
    • C.M. Liedtke Stability of actin cytoskeleton and PKC-delta binding to actin regulate NKCC1 function in airway epithelial cells Am. J. Physiol. Cell Physiol. 284 2003 C487 C496
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Liedtke, C.M.1
  • 42
    • 0142184475 scopus 로고    scopus 로고
    • PKCdelta inhibits PKCalpha-mediated activation of phospholipase D1 in a manner independent of its protein kinase activity
    • M. Oka PKCdelta inhibits PKCalpha-mediated activation of phospholipase D1 in a manner independent of its protein kinase activity FEBS Lett. 554 2003 179 183
    • (2003) FEBS Lett. , vol.554 , pp. 179-183
    • Oka, M.1
  • 43
    • 0037160074 scopus 로고    scopus 로고
    • Ligand-independent trans-activation of the platelet-derived growth factor receptor by reactive oxygen species requires protein kinase C-delta and c-Src
    • S. Saito Ligand-independent trans-activation of the platelet-derived growth factor receptor by reactive oxygen species requires protein kinase C-delta and c-Src J. Biol. Chem. 277 2002 44695 44700
    • (2002) J. Biol. Chem. , vol.277 , pp. 44695-44700
    • Saito, S.1
  • 44
    • 0041315639 scopus 로고    scopus 로고
    • Cholecystokinin-stimulated protein kinase C-delta kinase activation, tyrosine phosphorylation, and translocation are mediated by Src tyrosine kinases in pancreatic acinar cells
    • J.A. Tapia Cholecystokinin-stimulated protein kinase C-delta kinase activation, tyrosine phosphorylation, and translocation are mediated by Src tyrosine kinases in pancreatic acinar cells J. Biol. Chem. 278 2003 35220 35230
    • (2003) J. Biol. Chem. , vol.278 , pp. 35220-35230
    • Tapia, J.A.1
  • 45
    • 0036086234 scopus 로고    scopus 로고
    • A role for PKC-delta and PI 3-kinase in TNF-alpha-mediated antiapoptotic signaling in the human neutrophil
    • L.E. Kilpatrick A role for PKC-delta and PI 3-kinase in TNF-alpha-mediated antiapoptotic signaling in the human neutrophil Am. J. Physiol. Cell Physiol. 283 2002 C48 C57
    • (2002) Am. J. Physiol. Cell Physiol. , vol.283
    • Kilpatrick, L.E.1
  • 46
    • 0141918859 scopus 로고    scopus 로고
    • Pro-apoptotic protein kinase C delta is associated with intranuclear inclusions in a transgenic model of Huntington's disease
    • E.A. Zemskov Pro-apoptotic protein kinase C delta is associated with intranuclear inclusions in a transgenic model of Huntington's disease J. Neurochem. 87 2003 395 406
    • (2003) J. Neurochem. , vol.87 , pp. 395-406
    • Zemskov, E.A.1
  • 47
    • 0037147299 scopus 로고    scopus 로고
    • Protein kinase C delta associates with the interleukin-6 receptor subunit glycoprotein (gp) 130 via Stat3 and enhances Stat3-gp130 interaction
    • V. Novotny-Diermayr Protein kinase C delta associates with the interleukin-6 receptor subunit glycoprotein (gp) 130 via Stat3 and enhances Stat3-gp130 interaction J. Biol. Chem. 277 2002 49134 49142
    • (2002) J. Biol. Chem. , vol.277 , pp. 49134-49142
    • Novotny-Diermayr, V.1
  • 48
    • 0037189493 scopus 로고    scopus 로고
    • Selective association of protein kinase C with 14-3-3 zeta in neuronally differentiated PC12 Cells. Stimulatory and inhibitory effect of 14-3-3 zeta in vivo
    • L. Gannon-Murakami, and K. Murakami Selective association of protein kinase C with 14-3-3 zeta in neuronally differentiated PC12 Cells. Stimulatory and inhibitory effect of 14-3-3 zeta in vivo J. Biol. Chem. 277 2002 23116 23122
    • (2002) J. Biol. Chem. , vol.277 , pp. 23116-23122
    • Gannon-Murakami, L.1    Murakami, K.2
  • 49
    • 0345549478 scopus 로고    scopus 로고
    • Protein kinase Cepsilon interacts with Bax and promotes survival of human prostate cancer cells
    • M.A. McJilton Protein kinase Cepsilon interacts with Bax and promotes survival of human prostate cancer cells Oncogene 22 2003 7958 7968
    • (2003) Oncogene , vol.22 , pp. 7958-7968
    • McJilton, M.A.1
  • 50
    • 0037406848 scopus 로고    scopus 로고
    • A PKC epsilon-ENH-channel complex specifically modulates N-type Ca2+ channels
    • Y. Maeno-Hikichi A PKC epsilon-ENH-channel complex specifically modulates N-type Ca2+ channels Nat. Neurosci. 6 2003 468 475
    • (2003) Nat. Neurosci. , vol.6 , pp. 468-475
    • Maeno-Hikichi, Y.1
  • 51
    • 0037040343 scopus 로고    scopus 로고
    • Mitochondrial PKCepsilon and MAPK form signaling modules in the murine heart: Enhanced mitochondrial PKCepsilon-MAPK interactions and differential MAPK activation in PKCepsilon-induced cardioprotection
    • C.P. Baines Mitochondrial PKCepsilon and MAPK form signaling modules in the murine heart: enhanced mitochondrial PKCepsilon-MAPK interactions and differential MAPK activation in PKCepsilon-induced cardioprotection Circ. Res. 90 2002 390 397
    • (2002) Circ. Res. , vol.90 , pp. 390-397
    • Baines, C.P.1
  • 52
    • 0036005833 scopus 로고    scopus 로고
    • PKC epsilon is associated with myosin IIA and actin in fibroblasts
    • K. England PKC epsilon is associated with myosin IIA and actin in fibroblasts Cell. Signal. 14 2002 529 536
    • (2002) Cell. Signal. , vol.14 , pp. 529-536
    • England, K.1
  • 53
    • 1942454402 scopus 로고    scopus 로고
    • Role of a PDZ1 domain of NHERF1 in the binding of airway epithelial RACK1 to NHERF1
    • C.M. Liedtke Role of a PDZ1 domain of NHERF1 in the binding of airway epithelial RACK1 to NHERF1 Am. J. Physiol. Cell. Physiol. 286 2004 C1037 C1044
    • (2004) Am. J. Physiol. Cell. Physiol. , vol.286
    • Liedtke, C.M.1
  • 54
    • 0037177860 scopus 로고    scopus 로고
    • Nitric oxide (NO) induces nitration of protein kinase Cepsilon (PKCepsilon), facilitating PKCepsilon translocation via enhanced PKCepsilon -RACK2 interactions: A novel mechanism of no-triggered activation of PKCepsilon
    • Z. Balafanova Nitric oxide (NO) induces nitration of protein kinase Cepsilon (PKCepsilon), facilitating PKCepsilon translocation via enhanced PKCepsilon -RACK2 interactions: a novel mechanism of no-triggered activation of PKCepsilon J. Biol. Chem. 277 2002 15021 15027
    • (2002) J. Biol. Chem. , vol.277 , pp. 15021-15027
    • Balafanova, Z.1
  • 55
    • 0036081646 scopus 로고    scopus 로고
    • Molecular conformation dictates signaling module formation: Example of PKCepsilon and Src tyrosine kinase
    • C. Song Molecular conformation dictates signaling module formation: example of PKCepsilon and Src tyrosine kinase Am. J. Physiol. Heart Circ. Physiol. 282 2002 H1166 H1171
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.282
    • Song, C.1
  • 56
    • 0037968275 scopus 로고    scopus 로고
    • Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria
    • C.P. Baines Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria Circ. Res. 92 2003 873 880
    • (2003) Circ. Res. , vol.92 , pp. 873-880
    • Baines, C.P.1
  • 57
    • 0242414464 scopus 로고    scopus 로고
    • Rapid association of protein kinase C-epsilon with insulin granules is essential for insulin exocytosis
    • C.F. Mendez Rapid association of protein kinase C-epsilon with insulin granules is essential for insulin exocytosis J. Biol. Chem. 278 2003 44753 44757
    • (2003) J. Biol. Chem. , vol.278 , pp. 44753-44757
    • Mendez, C.F.1
  • 58
    • 0037151039 scopus 로고    scopus 로고
    • Protein kinase C epsilon-dependent regulation of cystic fibrosis transmembrane regulator involves binding to a receptor for activated C kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor
    • C.M. Liedtke Protein kinase C epsilon-dependent regulation of cystic fibrosis transmembrane regulator involves binding to a receptor for activated C kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor J. Biol. Chem. 277 2002 22925 22933
    • (2002) J. Biol. Chem. , vol.277 , pp. 22925-22933
    • Liedtke, C.M.1
  • 59
    • 0037077256 scopus 로고    scopus 로고
    • The anchoring protein RACK1 links protein kinase Cepsilon to integrin beta chains. Requirements for adhesion and motility
    • A. Besson The anchoring protein RACK1 links protein kinase Cepsilon to integrin beta chains. Requirements for adhesion and motility J. Biol. Chem. 277 2002 22073 22084
    • (2002) J. Biol. Chem. , vol.277 , pp. 22073-22084
    • Besson, A.1
  • 60
    • 0037099313 scopus 로고    scopus 로고
    • PKC epsilon controls the traffic of beta1 integrins in motile cells
    • J. Ivaska PKC epsilon controls the traffic of beta1 integrins in motile cells EMBO J. 21 2002 3608 3619
    • (2002) EMBO J. , vol.21 , pp. 3608-3619
    • Ivaska, J.1
  • 61
    • 0036314804 scopus 로고    scopus 로고
    • Association of protein kinase C with GABA(A) receptors containing alpha1 and alpha4 subunits in the cerebral cortex: Selective effects of chronic ethanol consumption
    • S. Kumar Association of protein kinase C with GABA(A) receptors containing alpha1 and alpha4 subunits in the cerebral cortex: selective effects of chronic ethanol consumption J. Neurochem. 82 2002 110 117
    • (2002) J. Neurochem. , vol.82 , pp. 110-117
    • Kumar, S.1
  • 62
    • 0037342547 scopus 로고    scopus 로고
    • Functional association of cytokine-induced SH2 protein and protein kinase C in activated T cells
    • S. Chen Functional association of cytokine-induced SH2 protein and protein kinase C in activated T cells Int. Immunol. 15 2003 403 409
    • (2003) Int. Immunol. , vol.15 , pp. 403-409
    • Chen, S.1
  • 63
    • 0141772457 scopus 로고    scopus 로고
    • Molecular recognition in dimerization between PB1 domains
    • Y. Noda Molecular recognition in dimerization between PB1 domains J. Biol. Chem. 278 2003 43516 43524
    • (2003) J. Biol. Chem. , vol.278 , pp. 43516-43524
    • Noda, Y.1
  • 64
    • 0346732291 scopus 로고    scopus 로고
    • Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation
    • E.J. Tisdale Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3- phosphate dehydrogenase phosphorylation J. Biol. Chem. 278 2003 52524 52530
    • (2003) J. Biol. Chem. , vol.278 , pp. 52524-52530
    • Tisdale, E.J.1
  • 65
    • 0141514011 scopus 로고    scopus 로고
    • Regulation of mature T lymphocyte proliferation and differentiation by Par-4
    • M.J. Lafuente Regulation of mature T lymphocyte proliferation and differentiation by Par-4 EMBO J. 22 2003 4689 4698
    • (2003) EMBO J. , vol.22 , pp. 4689-4698
    • Lafuente, M.J.1
  • 66
    • 0442325388 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis
    • A. Duran The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis Dev. Cell 6 2004 303 309
    • (2004) Dev. Cell , vol.6 , pp. 303-309
    • Duran, A.1
  • 67
    • 0042889451 scopus 로고    scopus 로고
    • PKC zeta participates in activation of inflammatory response induced by enteropathogenic E. coli
    • S.D. Savkovic PKC zeta participates in activation of inflammatory response induced by enteropathogenic E. coli Am. J. Physiol. Cell Physiol. 285 2003 C512 C521
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Savkovic, S.D.1
  • 68
    • 0037458703 scopus 로고    scopus 로고
    • ZIP3, a new splice variant of the PKC-zeta-interacting protein family, binds to GABAC receptors, PKC-zeta, and Kv beta 2
    • C. Croci ZIP3, a new splice variant of the PKC-zeta-interacting protein family, binds to GABAC receptors, PKC-zeta, and Kv beta 2 J. Biol. Chem. 278 2003 6128 6135
    • (2003) J. Biol. Chem. , vol.278 , pp. 6128-6135
    • Croci, C.1
  • 69
    • 1542375457 scopus 로고    scopus 로고
    • Association of CPI-17 with protein kinase C and casein kinase I
    • E. Zemlickova Association of CPI-17 with protein kinase C and casein kinase I Biochem. Biophys. Res. Commun. 316 2004 39 47
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 39-47
    • Zemlickova, E.1
  • 70
    • 0037085394 scopus 로고    scopus 로고
    • P32 (gC1qBP) is a general protein kinase C (PKC)-binding protein; Interaction and cellular localization of P32-PKC complexes in ray hepatocytes
    • M. Robles-Flores p32 (gC1qBP) is a general protein kinase C (PKC)-binding protein; interaction and cellular localization of P32-PKC complexes in ray hepatocytes J. Biol. Chem. 277 2002 5247 5255
    • (2002) J. Biol. Chem. , vol.277 , pp. 5247-5255
    • Robles-Flores, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.