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Volumn 1793, Issue 2, 2009, Pages 395-405

PKCδ-dependent functional switch of rpS3 between translation and DNA repair

Author keywords

Endonuclease activity; PKC ; rpS3; Src

Indexed keywords

ENDONUCLEASE; PROTEIN KINASE C THETA; RIBOSOME PROTEIN; PHOSPHOTYROSINE; PROTEIN KINASE C DELTA; PROTEIN TYROSINE KINASE; RIBOSOMAL PROTEIN S3;

EID: 58549107562     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.10.017     Document Type: Article
Times cited : (61)

References (66)
  • 1
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka Y. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334 (1988) 661-665
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 2
    • 0025751626 scopus 로고
    • Expression of protein kinase C genes in hemopoietic cells is cell-type- and B cell-differentiation stage specific
    • Mischak H., Kolch W., Goodnight J., Davidson W.F., Rapp U., Rose-John S., and Mushinski J.F. Expression of protein kinase C genes in hemopoietic cells is cell-type- and B cell-differentiation stage specific. J. Immunol. 147 (1991) 3981-3987
    • (1991) J. Immunol. , vol.147 , pp. 3981-3987
    • Mischak, H.1    Kolch, W.2    Goodnight, J.3    Davidson, W.F.4    Rapp, U.5    Rose-John, S.6    Mushinski, J.F.7
  • 4
    • 0026045711 scopus 로고
    • Structural and functional diversities of a family of signal transducing protein kinases, protein kinase C family; two distinct classes of PKC, conventional cPKC and novel nPKC
    • Ohno S., Akita Y., Hata A., Osada S., Kubo K., Konno Y., Akimoto K., Mizuno K., Saido T., Kuroki T., et al. Structural and functional diversities of a family of signal transducing protein kinases, protein kinase C family; two distinct classes of PKC, conventional cPKC and novel nPKC. Adv. Enzyme Regul. 31 (1991) 287-303
    • (1991) Adv. Enzyme Regul. , vol.31 , pp. 287-303
    • Ohno, S.1    Akita, Y.2    Hata, A.3    Osada, S.4    Kubo, K.5    Konno, Y.6    Akimoto, K.7    Mizuno, K.8    Saido, T.9    Kuroki, T.10
  • 5
    • 0028092237 scopus 로고
    • Selective involvement of protein kinase C isozymes in differentiation and neoplastic transformation
    • Goodnight J., Mischak H., and Mushinski J.F. Selective involvement of protein kinase C isozymes in differentiation and neoplastic transformation. Adv. Cancer Res. 64 (1994) 159-209
    • (1994) Adv. Cancer Res. , vol.64 , pp. 159-209
    • Goodnight, J.1    Mischak, H.2    Mushinski, J.F.3
  • 9
    • 0034677930 scopus 로고    scopus 로고
    • Interaction between protein kinase C delta and the c-Abl tyrosine kinase in the cellular response to oxidative stress
    • Sun X., Wu F., Datta R., Kharbanda S., and Kufe D. Interaction between protein kinase C delta and the c-Abl tyrosine kinase in the cellular response to oxidative stress. J. Biol. Chem. 275 (2000) 7470-7473
    • (2000) J. Biol. Chem. , vol.275 , pp. 7470-7473
    • Sun, X.1    Wu, F.2    Datta, R.3    Kharbanda, S.4    Kufe, D.5
  • 10
    • 0038237433 scopus 로고    scopus 로고
    • Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9
    • Yoshida K., Wang H.G., Miki Y., and Kufe D. Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9. EMBO J. 22 (2003) 1431-1441
    • (2003) EMBO J. , vol.22 , pp. 1431-1441
    • Yoshida, K.1    Wang, H.G.2    Miki, Y.3    Kufe, D.4
  • 11
    • 0033516666 scopus 로고    scopus 로고
    • Protein kinase C delta is essential for etoposide-induced apoptosis in salivary gland acinar cells
    • Reyland M.E., Anderson S.M., Matassa A.A., Barzen K.A., and Quissell D.O. Protein kinase C delta is essential for etoposide-induced apoptosis in salivary gland acinar cells. J. Biol. Chem. 274 (1999) 19115-19123
    • (1999) J. Biol. Chem. , vol.274 , pp. 19115-19123
    • Reyland, M.E.1    Anderson, S.M.2    Matassa, A.A.3    Barzen, K.A.4    Quissell, D.O.5
  • 12
    • 0030023982 scopus 로고    scopus 로고
    • Activation of protein kinase Cdelta in human myeloid leukemia cells treated with 1-beta-d-arabinofuranosylcytosine
    • Emoto Y., Kisaki H., Manome Y., Kharbanda S., and Kufe D. Activation of protein kinase Cdelta in human myeloid leukemia cells treated with 1-beta-d-arabinofuranosylcytosine. Blood 87 (1996) 1990-1996
    • (1996) Blood , vol.87 , pp. 1990-1996
    • Emoto, Y.1    Kisaki, H.2    Manome, Y.3    Kharbanda, S.4    Kufe, D.5
  • 13
    • 0037072483 scopus 로고    scopus 로고
    • p73beta is regulated by protein kinase Cdelta catalytic fragment generated in the apoptotic response to DNA damage
    • Ren J., Datta R., Shioya H., Li Y., Oki E., Biedermann V., Bharti A., and Kufe D. p73beta is regulated by protein kinase Cdelta catalytic fragment generated in the apoptotic response to DNA damage. J. Biol. Chem. 277 (2002) 33758-33765
    • (2002) J. Biol. Chem. , vol.277 , pp. 33758-33765
    • Ren, J.1    Datta, R.2    Shioya, H.3    Li, Y.4    Oki, E.5    Biedermann, V.6    Bharti, A.7    Kufe, D.8
  • 15
    • 0030976892 scopus 로고    scopus 로고
    • Association between v-Src and protein kinase C delta in v-Src-transformed fibroblasts
    • Zang Q., Lu Z., Curto M., Barile N., Shalloway D., and Foster D.A. Association between v-Src and protein kinase C delta in v-Src-transformed fibroblasts. J. Biol. Chem. 272 (1997) 13275-13280
    • (1997) J. Biol. Chem. , vol.272 , pp. 13275-13280
    • Zang, Q.1    Lu, Z.2    Curto, M.3    Barile, N.4    Shalloway, D.5    Foster, D.A.6
  • 17
    • 0031794093 scopus 로고    scopus 로고
    • Protein kinase C-delta activation and tyrosine phosphorylation in platelets
    • Moussazadeh M., and Haimovich B. Protein kinase C-delta activation and tyrosine phosphorylation in platelets. FEBS Lett. 438 (1998) 225-230
    • (1998) FEBS Lett. , vol.438 , pp. 225-230
    • Moussazadeh, M.1    Haimovich, B.2
  • 18
    • 0027942841 scopus 로고
    • Dissociation of phorbol esters leads to immediate redistribution to the cytosol of protein kinases C alpha and C delta in mouse keratinocytes
    • Szallasi Z., Smith C.B., and Blumberg P.M. Dissociation of phorbol esters leads to immediate redistribution to the cytosol of protein kinases C alpha and C delta in mouse keratinocytes. J. Biol. Chem. 269 (1994) 27159-27162
    • (1994) J. Biol. Chem. , vol.269 , pp. 27159-27162
    • Szallasi, Z.1    Smith, C.B.2    Blumberg, P.M.3
  • 20
    • 0036132855 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase Cdelta is essential for its apoptotic effect in response to etoposide
    • Blass M., Kronfeld I., Kazimirsky G., Blumberg P.M., and Brodie C. Tyrosine phosphorylation of protein kinase Cdelta is essential for its apoptotic effect in response to etoposide. Mol. Cell. Biol. 22 (2002) 182-195
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 182-195
    • Blass, M.1    Kronfeld, I.2    Kazimirsky, G.3    Blumberg, P.M.4    Brodie, C.5
  • 21
    • 0033082319 scopus 로고    scopus 로고
    • Protein kinase C delta
    • Gschwendt M. Protein kinase C delta. Eur. J. Biochem. 259 (1999) 555-564
    • (1999) Eur. J. Biochem. , vol.259 , pp. 555-564
    • Gschwendt, M.1
  • 22
    • 10944238407 scopus 로고    scopus 로고
    • Distinctive activation mechanisms and functions for protein kinase Cdelta
    • Steinberg S.F. Distinctive activation mechanisms and functions for protein kinase Cdelta. Biochem. J. 384 (2004) 449-459
    • (2004) Biochem. J. , vol.384 , pp. 449-459
    • Steinberg, S.F.1
  • 24
    • 1642263353 scopus 로고    scopus 로고
    • Involvement of protein kinase C-delta in DNA damage-induced apoptosis
    • Basu A. Involvement of protein kinase C-delta in DNA damage-induced apoptosis. J. Cell. Mol. Med. 7 (2003) 341-350
    • (2003) J. Cell. Mol. Med. , vol.7 , pp. 341-350
    • Basu, A.1
  • 25
    • 0142165230 scopus 로고    scopus 로고
    • The double life of ribosomal proteins
    • Zimmermann R.A. The double life of ribosomal proteins. Cell 115 (2003) 130-132
    • (2003) Cell , vol.115 , pp. 130-132
    • Zimmermann, R.A.1
  • 26
    • 0032972994 scopus 로고    scopus 로고
    • Involvement of ribosomal proteins in regulating cell growth and apoptosis: translational modulation or recruitment for extraribosomal activity?
    • Naora H. Involvement of ribosomal proteins in regulating cell growth and apoptosis: translational modulation or recruitment for extraribosomal activity?. Immunol. Cell Biol. 77 (1999) 197-205
    • (1999) Immunol. Cell Biol. , vol.77 , pp. 197-205
    • Naora, H.1
  • 27
    • 0029073989 scopus 로고
    • Implication of mammalian ribosomal protein S3 in the processing of DNA damage
    • Kim J., Chubatsu L.S., Admon A., Stahl J., Fellous R., and Linn S. Implication of mammalian ribosomal protein S3 in the processing of DNA damage. J. Biol. Chem. 270 (1995) 13620-13629
    • (1995) J. Biol. Chem. , vol.270 , pp. 13620-13629
    • Kim, J.1    Chubatsu, L.S.2    Admon, A.3    Stahl, J.4    Fellous, R.5    Linn, S.6
  • 28
    • 13744252138 scopus 로고    scopus 로고
    • Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3
    • Kim S.H., Lee J.Y., and Kim J. Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3. Biochem. Biophys. Res. Commun. 328 (2005) 962-967
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 962-967
    • Kim, S.H.1    Lee, J.Y.2    Kim, J.3
  • 29
    • 1342265497 scopus 로고    scopus 로고
    • RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis
    • Jang C.Y., Lee J.Y., and Kim J. RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis. FEBS Lett. 560 (2004) 81-85
    • (2004) FEBS Lett. , vol.560 , pp. 81-85
    • Jang, C.Y.1    Lee, J.Y.2    Kim, J.3
  • 31
    • 33746956118 scopus 로고    scopus 로고
    • Reduction of invasion in human fibrosarcoma cells by ribosomal protein S3 in conjunction with Nm23-H1 and ERK
    • Kim S.H., and Kim J. Reduction of invasion in human fibrosarcoma cells by ribosomal protein S3 in conjunction with Nm23-H1 and ERK. Biochim. Biophys. Acta 1763 8 (2006) 823-832
    • (2006) Biochim. Biophys. Acta , vol.1763 , Issue.8 , pp. 823-832
    • Kim, S.H.1    Kim, J.2
  • 32
    • 31944445649 scopus 로고    scopus 로고
    • Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation
    • Kim T.S., Jang C.Y., Kim H.D., Lee J.Y., Ahn B.Y., and Kim J. Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation. Mol. Biol. Cell 17 (2006) 824-833
    • (2006) Mol. Biol. Cell , vol.17 , pp. 824-833
    • Kim, T.S.1    Jang, C.Y.2    Kim, H.D.3    Lee, J.Y.4    Ahn, B.Y.5    Kim, J.6
  • 33
    • 33745228890 scopus 로고    scopus 로고
    • Hrr25-dependent phosphorylation state regulates organization of the pre-40S subunit
    • Schafer T., Maco B., Petfalski E., Tollervey D., Bottcher B., Aebi U., and Hurt E. Hrr25-dependent phosphorylation state regulates organization of the pre-40S subunit. Nature 441 (2006) 651-655
    • (2006) Nature , vol.441 , pp. 651-655
    • Schafer, T.1    Maco, B.2    Petfalski, E.3    Tollervey, D.4    Bottcher, B.5    Aebi, U.6    Hurt, E.7
  • 34
    • 0142227209 scopus 로고    scopus 로고
    • Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control
    • Mazumder B., Sampath P., Seshadri V., Maitra R.K., DiCorleto P.E., and Fox P.L. Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control. Cell 115 (2003) 187-198
    • (2003) Cell , vol.115 , pp. 187-198
    • Mazumder, B.1    Sampath, P.2    Seshadri, V.3    Maitra, R.K.4    DiCorleto, P.E.5    Fox, P.L.6
  • 35
    • 0033523114 scopus 로고    scopus 로고
    • Co-translational assembly of the D1 protein into photosystem II
    • Zhang L., Paakkarinen V., van Wijk K.J., and Aro E.M. Co-translational assembly of the D1 protein into photosystem II. J. Biol. Chem. 274 (1999) 16062-16067
    • (1999) J. Biol. Chem. , vol.274 , pp. 16062-16067
    • Zhang, L.1    Paakkarinen, V.2    van Wijk, K.J.3    Aro, E.M.4
  • 36
    • 20444432227 scopus 로고    scopus 로고
    • Erk phosphorylates threonine 42 residue of ribosomal protein S3
    • Kim H.D., Lee J.Y., and Kim J. Erk phosphorylates threonine 42 residue of ribosomal protein S3. Biochem. Biophys. Res. Commun. 333 (2005) 110-115
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 110-115
    • Kim, H.D.1    Lee, J.Y.2    Kim, J.3
  • 38
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil S.A., Villen J., Gerber S.A., Rush J., and Gygi S.P. A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat. Biotechnol. 24 (2006) 1285-1292
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 40
    • 0031570118 scopus 로고    scopus 로고
    • Phosphorylation and subcellular redistribution of pleckstrin in human neutrophils
    • Brumell J.H., Craig K.L., Ferguson D., Tyers M., and Grinstein S. Phosphorylation and subcellular redistribution of pleckstrin in human neutrophils. J. Immunol. 158 (1997) 4862-4871
    • (1997) J. Immunol. , vol.158 , pp. 4862-4871
    • Brumell, J.H.1    Craig, K.L.2    Ferguson, D.3    Tyers, M.4    Grinstein, S.5
  • 42
    • 0033233483 scopus 로고    scopus 로고
    • Protein kinase Cdelta targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector
    • Li L., Lorenzo P.S., Bogi K., Blumberg P.M., and Yuspa S.H. Protein kinase Cdelta targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector. Mol. Cell. Biol. 19 (1999) 8547-8558
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8547-8558
    • Li, L.1    Lorenzo, P.S.2    Bogi, K.3    Blumberg, P.M.4    Yuspa, S.H.5
  • 43
    • 21244479797 scopus 로고    scopus 로고
    • Roles of tyrosine phosphorylation and cleavage of protein kinase Cdelta in its protective effect against tumor necrosis factor-related apoptosis inducing ligand-induced apoptosis
    • Okhrimenko H., Lu W., Xiang C., Ju D., Blumberg P.M., Gomel R., Kazimirsky G., and Brodie C. Roles of tyrosine phosphorylation and cleavage of protein kinase Cdelta in its protective effect against tumor necrosis factor-related apoptosis inducing ligand-induced apoptosis. J. Biol. Chem. 280 (2005) 23643-23652
    • (2005) J. Biol. Chem. , vol.280 , pp. 23643-23652
    • Okhrimenko, H.1    Lu, W.2    Xiang, C.3    Ju, D.4    Blumberg, P.M.5    Gomel, R.6    Kazimirsky, G.7    Brodie, C.8
  • 44
    • 34249006580 scopus 로고    scopus 로고
    • Protein kinase C delta negatively regulates tyrosine hydroxylase activity and dopamine synthesis by enhancing protein phosphatase-2A activity in dopaminergic neurons
    • Zhang D., Kanthasamy A., Yang Y., and Anantharam V. Protein kinase C delta negatively regulates tyrosine hydroxylase activity and dopamine synthesis by enhancing protein phosphatase-2A activity in dopaminergic neurons. J. Neurosci. 27 (2007) 5349-5362
    • (2007) J. Neurosci. , vol.27 , pp. 5349-5362
    • Zhang, D.1    Kanthasamy, A.2    Yang, Y.3    Anantharam, V.4
  • 46
    • 0034989803 scopus 로고    scopus 로고
    • Modulation of PKCdelta tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases
    • Benes C., and Soltoff S.P. Modulation of PKCdelta tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases. Am. J. Physiol., Cell Physiol. 280 (2001) C1498-1510
    • (2001) Am. J. Physiol., Cell Physiol. , vol.280
    • Benes, C.1    Soltoff, S.P.2
  • 47
    • 0029924152 scopus 로고    scopus 로고
    • Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C delta
    • Denning M.F., Dlugosz A.A., Threadgill D.W., Magnuson T., and Yuspa S.H. Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C delta. J. Biol. Chem. 271 (1996) 5325-5331
    • (1996) J. Biol. Chem. , vol.271 , pp. 5325-5331
    • Denning, M.F.1    Dlugosz, A.A.2    Threadgill, D.W.3    Magnuson, T.4    Yuspa, S.H.5
  • 49
    • 0033367325 scopus 로고    scopus 로고
    • Ribosome synthesis in Saccharomyces cerevisiae
    • Venema J., and Tollervey D. Ribosome synthesis in Saccharomyces cerevisiae. Annu. Rev. Genet. 33 (1999) 261-311
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 261-311
    • Venema, J.1    Tollervey, D.2
  • 50
    • 0142025159 scopus 로고    scopus 로고
    • PKCdelta-dependent cleavage and nuclear translocation of annexin A1 by phorbol 12-myristate 13-acetate
    • Kim Y.S., Ko J., Kim I.S., Jang S.W., Sung H.J., Lee H.J., Lee S.Y., Kim Y., and Na D.S. PKCdelta-dependent cleavage and nuclear translocation of annexin A1 by phorbol 12-myristate 13-acetate. Eur. J. Biochem. 270 (2003) 4089-4094
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4089-4094
    • Kim, Y.S.1    Ko, J.2    Kim, I.S.3    Jang, S.W.4    Sung, H.J.5    Lee, H.J.6    Lee, S.Y.7    Kim, Y.8    Na, D.S.9
  • 51
    • 23744476859 scopus 로고    scopus 로고
    • Impact of PKCdelta on estrogen receptor localization and activity in breast cancer cells
    • De Servi B., Hermani A., Medunjanin S., and Mayer D. Impact of PKCdelta on estrogen receptor localization and activity in breast cancer cells. Oncogene 24 (2005) 4946-4955
    • (2005) Oncogene , vol.24 , pp. 4946-4955
    • De Servi, B.1    Hermani, A.2    Medunjanin, S.3    Mayer, D.4
  • 53
    • 0029789967 scopus 로고    scopus 로고
    • Protein kinase C activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf
    • Ueda Y., Hirai S., Osada S., Suzuki A., Mizuno K., and Ohno S. Protein kinase C activates the MEK-ERK pathway in a manner independent of Ras and dependent on Raf. J. Biol. Chem. 271 (1996) 23512-23519
    • (1996) J. Biol. Chem. , vol.271 , pp. 23512-23519
    • Ueda, Y.1    Hirai, S.2    Osada, S.3    Suzuki, A.4    Mizuno, K.5    Ohno, S.6
  • 54
    • 0037151034 scopus 로고    scopus 로고
    • Mechanism of 17-beta-estradiol-induced Erk1/2 activation in breast cancer cells. A role for HER2 AND PKC-delta
    • Keshamouni V.G., Mattingly R.R., and Reddy K.B. Mechanism of 17-beta-estradiol-induced Erk1/2 activation in breast cancer cells. A role for HER2 AND PKC-delta. J. Biol. Chem. 277 (2002) 22558-22565
    • (2002) J. Biol. Chem. , vol.277 , pp. 22558-22565
    • Keshamouni, V.G.1    Mattingly, R.R.2    Reddy, K.B.3
  • 55
    • 0020484358 scopus 로고
    • Influence of the state of ribosome association on the phosphorylation of ribosomal proteins in isolated ribosome-protein kinase systems from rat cerebral cortex
    • Francis T.A., and Roberts S. Influence of the state of ribosome association on the phosphorylation of ribosomal proteins in isolated ribosome-protein kinase systems from rat cerebral cortex. Biochem. J. 208 (1982) 289-300
    • (1982) Biochem. J. , vol.208 , pp. 289-300
    • Francis, T.A.1    Roberts, S.2
  • 56
    • 0015972852 scopus 로고
    • A kinase that transfers the gamma-phosphoryl group of GTP to proteins of eukaryotic 40S ribosomal subunits
    • Ventimiglia F.A., and Wool I.G. A kinase that transfers the gamma-phosphoryl group of GTP to proteins of eukaryotic 40S ribosomal subunits. Proc. Natl. Acad. Sci. U. S. A. 71 (1974) 350-354
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 350-354
    • Ventimiglia, F.A.1    Wool, I.G.2
  • 57
    • 0025719209 scopus 로고
    • Phosphorylation controls binding of acidic proteins to the ribosome
    • Naranda T., and Ballesta J.P. Phosphorylation controls binding of acidic proteins to the ribosome. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 10563-10567
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10563-10567
    • Naranda, T.1    Ballesta, J.P.2
  • 58
    • 0035878872 scopus 로고    scopus 로고
    • Regulation of a G protein-gated inwardly rectifying K+ channel by a Ca(2+)-independent protein kinase C
    • Leaney J.L., Dekker L.V., and Tinker A. Regulation of a G protein-gated inwardly rectifying K+ channel by a Ca(2+)-independent protein kinase C. J. Physiol. 534 (2001) 367-379
    • (2001) J. Physiol. , vol.534 , pp. 367-379
    • Leaney, J.L.1    Dekker, L.V.2    Tinker, A.3
  • 59
    • 0026825333 scopus 로고
    • Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart
    • Bacher N., Zisman Y., Berent E., and Livneh E. Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart. Mol. Cell. Biol. 12 (1992) 1404
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1404
    • Bacher, N.1    Zisman, Y.2    Berent, E.3    Livneh, E.4
  • 60
    • 34548541557 scopus 로고    scopus 로고
    • Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress
    • (Amst.)
    • Yadavilli S., Hegde V., and Deutsch W.A. Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress. DNA Repair 6 (2007) 1453-1462 (Amst.)
    • (2007) DNA Repair , vol.6 , pp. 1453-1462
    • Yadavilli, S.1    Hegde, V.2    Deutsch, W.A.3
  • 63
    • 11244296193 scopus 로고    scopus 로고
    • Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity
    • Coin F., Auriol J., Tapias A., Clivio P., Vermeulen W., and Egly J.M. Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity. EMBO J. 23 (2004) 4835-4846
    • (2004) EMBO J. , vol.23 , pp. 4835-4846
    • Coin, F.1    Auriol, J.2    Tapias, A.3    Clivio, P.4    Vermeulen, W.5    Egly, J.M.6
  • 64
    • 0242721592 scopus 로고    scopus 로고
    • Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway
    • Zhang Y., Wolf G.W., Bhat K., Jin A., Allio T., Burkhart W.A., and Xiong Y. Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway. Mol. Cell. Biol. 23 (2003) 8902-8912
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8902-8912
    • Zhang, Y.1    Wolf, G.W.2    Bhat, K.3    Jin, A.4    Allio, T.5    Burkhart, W.A.6    Xiong, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.