메뉴 건너뛰기




Volumn 406, Issue , 2006, Pages 234-250

Purification and kinase assay of PKN

Author keywords

[No Author keywords available]

Indexed keywords

ISOENZYME; PROTEIN KINASE C; PROTEIN SERINE THREONINE KINASE;

EID: 32144462081     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(06)06017-4     Document Type: Review
Times cited : (10)

References (36)
  • 2
    • 0033780417 scopus 로고    scopus 로고
    • Purification and in vitro activity of Rho-associated kinase
    • Amano M., Fukata Y., Shimokawa H., and Kaibuchi K. Purification and in vitro activity of Rho-associated kinase Methods Enzymol. 325 2000 149 155
    • (2000) Methods Enzymol. , vol.325 , pp. 149-155
    • Amano, M.1    Fukata, Y.2    Shimokawa, H.3    Kaibuchi, K.4
  • 4
    • 0034624990 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton
    • Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., and Liu F. Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton Proc. Natl. Acad. Sci. USA 97 2000 5089 5094
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5089-5094
    • Dong, L.Q.1    Landa, L.R.2    Wick, M.J.3    Zhu, L.4    Mukai, H.5    Ono, Y.6    Liu, F.7
  • 5
    • 0022341259 scopus 로고
    • Activation of protein kinase C by Triton X-100 mixed micelles containing diacylglycerol and phosphatidylserine
    • Hannun Y.A., Loomis C.R., and Bell R.M. Activation of protein kinase C by Triton X-100 mixed micelles containing diacylglycerol and phosphatidylserine J. Biol. Chem. 260 1985 10039 10043
    • (1985) J. Biol. Chem. , vol.260 , pp. 10039-10043
    • Hannun, Y.A.1    Loomis, C.R.2    Bell, R.M.3
  • 6
    • 0343852701 scopus 로고    scopus 로고
    • Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: A detoxification enzyme and fusion-protein affinity tag
    • Kaplan W., Husler P., Klump H., Erhardt J., Sluis-Cremer N., and Dirr H. Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag Protein Sci. 6 1997 399 406
    • (1997) Protein Sci. , vol.6 , pp. 399-406
    • Kaplan, W.1    Husler, P.2    Klump, H.3    Erhardt, J.4    Sluis-Cremer, N.5    Dirr, H.6
  • 7
    • 0029048334 scopus 로고
    • Purification and characterization of a fatty acid-activated protein kinase (PKN) from rat testis
    • Kitagawa M., Mukai H., Shibata H., and Ono Y. Purification and characterization of a fatty acid-activated protein kinase (PKN) from rat testis Biochem. J. 310 Pt 2 1995 657 664
    • (1995) Biochem. J. , vol.310 , Issue.2 PART , pp. 657-664
    • Kitagawa, M.1    Mukai, H.2    Shibata, H.3    Ono, Y.4
  • 8
    • 14044266297 scopus 로고    scopus 로고
    • Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter
    • Kunkel M.T., Ni Q., Tsien R.Y., Zhang J., and Newton A.C. Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter J. Biol. Chem. 280 2005 5581 5587
    • (2005) J. Biol. Chem. , vol.280 , pp. 5581-5587
    • Kunkel, M.T.1    Ni, Q.2    Tsien, R.Y.3    Zhang, J.4    Newton, A.C.5
  • 13
    • 0028145594 scopus 로고
    • Differential effects of fatty acid and phospholipid activators on the catalytic activities of a structurally novel protein kinase from rat liver
    • Morrice N.A., Fecondo J., and Wettenhall R.E. Differential effects of fatty acid and phospholipid activators on the catalytic activities of a structurally novel protein kinase from rat liver FEBS Lett. 351 1994 171 175
    • (1994) FEBS Lett. , vol.351 , pp. 171-175
    • Morrice, N.A.1    Fecondo, J.2    Wettenhall, R.E.3
  • 14
    • 0027930897 scopus 로고
    • A cardiolipin-activated protein kinase from rat liver structurally distinct from the protein kinases C
    • Morrice N.A., Gabrielli B., Kemp B.E., and Wettenhall R.E. A cardiolipin-activated protein kinase from rat liver structurally distinct from the protein kinases C J. Biol. Chem. 269 1994 20040 20046
    • (1994) J. Biol. Chem. , vol.269 , pp. 20040-20046
    • Morrice, N.A.1    Gabrielli, B.2    Kemp, B.E.3    Wettenhall, R.E.4
  • 15
    • 0028260527 scopus 로고
    • A novel protein kinase with leucine zipper-like sequences: Its catalytic domain is highly homologous to that of protein kinase C
    • Mukai H., and Ono Y. A novel protein kinase with leucine zipper-like sequences: Its catalytic domain is highly homologous to that of protein kinase C Biochem. Biophys. Res. Commun. 199 1994 897 904
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 897-904
    • Mukai, H.1    Ono, Y.2
  • 17
    • 0037283966 scopus 로고    scopus 로고
    • The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC
    • Mukai H. The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC J. Biochem. (Tokyo) 133 2003 17 27
    • (2003) J. Biochem. (Tokyo) , vol.133 , pp. 17-27
    • Mukai, H.1
  • 19
    • 1542442707 scopus 로고    scopus 로고
    • Expression and purification of protein kinase C from insect cells
    • Mukai H., and Ono Y. Expression and purification of protein kinase C from insect cells Methods Mol. Biol. 233 2003 21 34
    • (2003) Methods Mol. Biol. , vol.233 , pp. 21-34
    • Mukai, H.1    Ono, Y.2
  • 21
    • 0033546497 scopus 로고    scopus 로고
    • Identification and characterization of PKNbeta, a novel isoform of protein kinase PKN: Expression and arachidonic acid dependency are different from those of PKNalpha
    • Oishi K., Mukai H., Shibata H., Takahashi M., and Ono Y. Identification and characterization of PKNbeta, a novel isoform of protein kinase PKN: Expression and arachidonic acid dependency are different from those of PKNalpha Biochem. Biophys. Res. Commun. 261 1999 808 814
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 808-814
    • Oishi, K.1    Mukai, H.2    Shibata, H.3    Takahashi, M.4    Ono, Y.5
  • 22
    • 0029091623 scopus 로고
    • Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. a comparison with protein kinase C isotypes
    • Palmer R.H., Dekker L.V., Woscholski R., Le Good J.A., Gigg R., and Parker P.J. Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes J. Biol. Chem. 270 1995 22412 22416
    • (1995) J. Biol. Chem. , vol.270 , pp. 22412-22416
    • Palmer, R.H.1    Dekker, L.V.2    Woscholski, R.3    Le Good, J.A.4    Gigg, R.5    Parker, P.J.6
  • 23
    • 0028815490 scopus 로고
    • Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family
    • Palmer R.H., Ridden J., and Parker P.J. Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family Eur. J. Biochem. 227 1995 344 351
    • (1995) Eur. J. Biochem. , vol.227 , pp. 344-351
    • Palmer, R.H.1    Ridden, J.2    Parker, P.J.3
  • 25
    • 0029731347 scopus 로고    scopus 로고
    • Phosphorylation events associated with different states of activation of a hepatic cardiolipin/protease-activated protein kinase. Structural identity to the protein kinase N-type protein kinases
    • Peng B., Morrice N.A., Groenen L.C., and Wettenhall R.E. Phosphorylation events associated with different states of activation of a hepatic cardiolipin/protease-activated protein kinase. Structural identity to the protein kinase N-type protein kinases J. Biol. Chem. 271 1996 32233 32240
    • (1996) J. Biol. Chem. , vol.271 , pp. 32233-32240
    • Peng, B.1    Morrice, N.A.2    Groenen, L.C.3    Wettenhall, R.E.4
  • 26
    • 0036196296 scopus 로고    scopus 로고
    • Fluorescent indicators for imaging protein phosphorylation in single living cells
    • Sato M., Ozawa T., Inukai K., Asano T., and Umezawa Y. Fluorescent indicators for imaging protein phosphorylation in single living cells Nat. Biotechnol. 20 2002 287 294
    • (2002) Nat. Biotechnol. , vol.20 , pp. 287-294
    • Sato, M.1    Ozawa, T.2    Inukai, K.3    Asano, T.4    Umezawa, Y.5
  • 27
  • 28
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • Ting A.Y., Kain K.H., Klemke R.L., and Tsien R.Y. Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells Proc. Natl. Acad. Sci. USA 98 2001 15003 15008
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15003-15008
    • Ting, A.Y.1    Kain, K.H.2    Klemke, R.L.3    Tsien, R.Y.4
  • 29
    • 0041355220 scopus 로고    scopus 로고
    • Hyperosmotic-induced protein kinase N 1 activation in a vesicular compartment is dependent upon Rac1 and 3-phosphoinositide-dependent kinase 1
    • Torbett N.E., Casamassima A., and Parker P.J. Hyperosmotic-induced protein kinase N 1 activation in a vesicular compartment is dependent upon Rac1 and 3-phosphoinositide-dependent kinase 1 J. Biol. Chem. 278 2003 32344 32351
    • (2003) J. Biol. Chem. , vol.278 , pp. 32344-32351
    • Torbett, N.E.1    Casamassima, A.2    Parker, P.J.3
  • 30
    • 0030894714 scopus 로고    scopus 로고
    • The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization
    • Vincent S., and Settleman J. The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization Mol. Cell Biol. 17 1997 2247 2256
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2247-2256
    • Vincent, S.1    Settleman, J.2
  • 31
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • Violin J.D., Zhang J., Tsien R.Y., and Newton A.C. A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C J. Cell Biol. 161 2003 899 909
    • (2003) J. Cell Biol. , vol.161 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 33
    • 0037219041 scopus 로고    scopus 로고
    • Endogenous mono-ADP-ribosylation mediates smooth muscle cell proliferation and migration via protein kinase N-dependent induction of c-fos expression
    • Yau L., Litchie B., Thomas S., Storie B., Yurkova N., and Zahradka P. Endogenous mono-ADP-ribosylation mediates smooth muscle cell proliferation and migration via protein kinase N-dependent induction of c-fos expression Eur. J. Biochem. 270 2003 101 110
    • (2003) Eur. J. Biochem. , vol.270 , pp. 101-110
    • Yau, L.1    Litchie, B.2    Thomas, S.3    Storie, B.4    Yurkova, N.5    Zahradka, P.6
  • 34
    • 0032826336 scopus 로고    scopus 로고
    • Mutational analysis of the regulatory mechanism of PKN: The regulatory region of PKN contains an arachidonic acid-sensitive autoinhibitory domain
    • Yoshinaga C., Mukai H., Toshimori M., Miyamoto M., and Ono Y. Mutational analysis of the regulatory mechanism of PKN: the regulatory region of PKN contains an arachidonic acid-sensitive autoinhibitory domain J. Biochem. (Tokyo) 126 1999 475 484
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 475-484
    • Yoshinaga, C.1    Mukai, H.2    Toshimori, M.3    Miyamoto, M.4    Ono, Y.5
  • 35
    • 0030980027 scopus 로고    scopus 로고
    • Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities
    • Yu W., Liu J., Morrice N.A., and Wettenhall R.E. Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities J. Biol. Chem. 272 1997 10030 10034
    • (1997) J. Biol. Chem. , vol.272 , pp. 10030-10034
    • Yu, W.1    Liu, J.2    Morrice, N.A.3    Wettenhall, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.