메뉴 건너뛰기




Volumn 347, Issue 4, 2006, Pages 1166-1170

Phosphorylation of transglutaminase 2 by PKA at Ser216 creates 14-3-3 binding sites

Author keywords

14 3 3; BH3 domain; Phosphorylation; PKA; Transglutaminase 2

Indexed keywords

ANTISERUM; CYCLIC AMP DEPENDENT PROTEIN KINASE; PEPTIDE; PROTEIN 14 3 3; PROTEIN ANTIBODY; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRANSGLUTAMINASE 2; UNCLASSIFIED DRUG;

EID: 33746347678     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.07.041     Document Type: Article
Times cited : (24)

References (22)
  • 1
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: an enigmatic enzyme with diverse functions
    • Fesus L., and Piacentini M. Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem. Sci. 27 (2002) 534-539
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 2
    • 2642536093 scopus 로고    scopus 로고
    • Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor binding protein-3 kinase
    • Mishra S., and Murphy L.J. Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor binding protein-3 kinase. J. Biol. Chem. 279 (2004) 23863-23868
    • (2004) J. Biol. Chem. , vol.279 , pp. 23863-23868
    • Mishra, S.1    Murphy, L.J.2
  • 4
    • 0028176166 scopus 로고
    • Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka H., Perez D.M., Baek K.J., Das T., husain A., Misono K., Im M.J., and Graham R.M. Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science 264 (1994) 1593-1596
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    husain, A.5    Misono, K.6    Im, M.J.7    Graham, R.M.8
  • 5
    • 33746328129 scopus 로고    scopus 로고
    • S. Mishra, G. Melino, L.J. Murphy, Transglutaminase 2 kinase activity facilitates protein kinase A induced phosphorylation of retinoblastoma protein (unpublished observation).
  • 7
    • 0142106382 scopus 로고    scopus 로고
    • Chondrocyte-derived transglutaminase promotes maturation of preosteoblasts in periosteal bone
    • Nurminskaya M., Magee C., Faverman L., and Linsenmayer T.F. Chondrocyte-derived transglutaminase promotes maturation of preosteoblasts in periosteal bone. Dev. Biol. 263 (2003) 139-152
    • (2003) Dev. Biol. , vol.263 , pp. 139-152
    • Nurminskaya, M.1    Magee, C.2    Faverman, L.3    Linsenmayer, T.F.4
  • 8
    • 33644932810 scopus 로고    scopus 로고
    • Prohibitin attenuates insulin-stimulated glucose and fatty acid oxidation in adipose tissue by inhibition of pyruvate carboxylase
    • Vessal M., Mishra S., Moulik S., and Murphy L.J. Prohibitin attenuates insulin-stimulated glucose and fatty acid oxidation in adipose tissue by inhibition of pyruvate carboxylase. FEBS J. 273 (2006) 568-576
    • (2006) FEBS J. , vol.273 , pp. 568-576
    • Vessal, M.1    Mishra, S.2    Moulik, S.3    Murphy, L.J.4
  • 10
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin A.J., Tanner J.W., Allen P.M., and Shaw A.S. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84 6 (1996) 889-897
    • (1996) Cell , vol.84 , Issue.6 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 11
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe M.B. How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513 (2002) 53-57
    • (2002) FEBS Lett. , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 12
    • 0030827138 scopus 로고    scopus 로고
    • Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta protein
    • Zhang S.H., Kobayashi R., Graves P.R., Piwnica-Worms H., and Tonks N.K. Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta protein. J. Biol. Chem. 272 (1997) 27281-27287
    • (1997) J. Biol. Chem. , vol.272 , pp. 27281-27287
    • Zhang, S.H.1    Kobayashi, R.2    Graves, P.R.3    Piwnica-Worms, H.4    Tonks, N.K.5
  • 13
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J., Harada H., Yang E., Jockel J., and Korsmeyer S.J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 87 (1996) 619-628
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 14
    • 0032190082 scopus 로고    scopus 로고
    • Replication checkpoint requires phosphorylation of the phosphatase Cdc25 by Cds1 or Chk1
    • Zeng Y., Forbes K.C., Wu Z., Moreno S., Piwnica-Worms H., and Enoch T. Replication checkpoint requires phosphorylation of the phosphatase Cdc25 by Cds1 or Chk1. Nature 395 (1998) 507-510
    • (1998) Nature , vol.395 , pp. 507-510
    • Zeng, Y.1    Forbes, K.C.2    Wu, Z.3    Moreno, S.4    Piwnica-Worms, H.5    Enoch, T.6
  • 15
    • 33646903670 scopus 로고    scopus 로고
    • Dynamic 14-3-3/client protein interactions integrate survival and apoptotic pathways
    • Porter G.W., Khuri F.R., and Fu H. Dynamic 14-3-3/client protein interactions integrate survival and apoptotic pathways. Semin. Cancer Biol. 16 (2006) 193-202
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 193-202
    • Porter, G.W.1    Khuri, F.R.2    Fu, H.3
  • 16
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh C. Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem. J. 381 (2004) 329-342
    • (2004) Biochem. J. , vol.381 , pp. 329-342
    • Mackintosh, C.1
  • 17
    • 0033635235 scopus 로고    scopus 로고
    • 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation
    • Datta S.R., Katsov A., Hu L., Petros A., Fesik S.W., Yaffe M.B., and Greenberg M.E. 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. Mol. Cell. 6 (2000) 41-51
    • (2000) Mol. Cell. , vol.6 , pp. 41-51
    • Datta, S.R.1    Katsov, A.2    Hu, L.3    Petros, A.4    Fesik, S.W.5    Yaffe, M.B.6    Greenberg, M.E.7
  • 18
    • 33644865025 scopus 로고    scopus 로고
    • Evidence that Ser87 of BimEL is phosphorylated by Akt and regulates BimEL apoptotic function
    • Qi X.J., Wildey G.M., and Howe P.H. Evidence that Ser87 of BimEL is phosphorylated by Akt and regulates BimEL apoptotic function. J. Biol. Chem. 281 (2006) 813-823
    • (2006) J. Biol. Chem. , vol.281 , pp. 813-823
    • Qi, X.J.1    Wildey, G.M.2    Howe, P.H.3
  • 19
    • 32944458740 scopus 로고    scopus 로고
    • Pim kinases phosphorylated multiple sites on Bad and promote 14-3-3 binding and dissociation from Bcl-XL
    • Macdonald A., Campbell D.G., Toth R., McLauchlan H., Hastie C.J., and Arthur J.S. Pim kinases phosphorylated multiple sites on Bad and promote 14-3-3 binding and dissociation from Bcl-XL. BMC Cell Biol. 7 (2006) 1
    • (2006) BMC Cell Biol. , vol.7 , pp. 1
    • Macdonald, A.1    Campbell, D.G.2    Toth, R.3    McLauchlan, H.4    Hastie, C.J.5    Arthur, J.S.6
  • 21
    • 33646942156 scopus 로고    scopus 로고
    • Regulation of the p53-MDM2 pathway by 14-3-3 sigma and other proteins
    • Lee M.H., and Lozano G. Regulation of the p53-MDM2 pathway by 14-3-3 sigma and other proteins. Semin. Cancer Biol. 16 (2006) 225-234
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 225-234
    • Lee, M.H.1    Lozano, G.2
  • 22
    • 28444488402 scopus 로고    scopus 로고
    • The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity
    • Mishra S., and Murphy L.J. The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity. Biochem. Biophy. Res. Comm. 339 (2006) 726-730
    • (2006) Biochem. Biophy. Res. Comm. , vol.339 , pp. 726-730
    • Mishra, S.1    Murphy, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.