caa a22 4500 477120377 CHVBK 20180405111635.0 cr unu---uuuuu 170330e19961201xx s 000 0 eng 10.1007/BF00229744 doi (NATIONALLICENCE)springer-10.1007/BF00229744 Glycogen synthase kinase 3 phosphorylation of different residues in the presence of different factors: Analysis on tau protein [Elektronische Daten] [Francisco Moreno, J. Muñoz-Montaño, Jesús Avila] Several peptides derived from microtubule-associated tau protein, have been tested as substrates for glycogen synthase kinase 3 (GSK 3). In the absence of cofactors, GSK 3 can modify serines or threonines followed by prolines. In other cases, a phosphorylation in position +4 is required for the phosphorylation of threonine/serine residues. A third type of substrate can be modified by GSK 3 in the presence of heparin. The comparison of GSK 3 with other kinases suggests some similar features of this kinase with proline-directed protein kinases, such as cdc-2 or mitogen-activated protein kinase (MAP Kinases) and also with casein kinase 2 (CK 2). Thus, all these kinases are specifically inhibited by 5,6-Dichloro-1-β-D-ribofuranosyl)-benzimidazole (DRB). However, heparin is an inhibitor of CK 2 whereas it activates the modification of certain substrates by GSK 3. A possible explanation for the obtained results is that the consensus sequence for GSK 3 phosphorylation is a serine/ threonine adjacent to a proline or other β-turn former residue and that such recognition could be favoured by the presence of adjacent negative charges or the addition of polyanions. Kluwer Academic Publishers, 1996 glycogen synthase kinase 3 nationallicence substrate consensus sequence nationallicence tau protein nationallicence GSK 3 : glycogen synthase kinase 3 nationallicence PDPK : proline-directed protein kinase nationallicence DRB : 5,6-Dichloro-1-β-Dribofuranosyl)benzimidazole nationallicence Moreno Francisco Centro de Biología Molecular ‘Severo Ochoa', Universidad Autónoma de Madrid, 28049, Cantoblanco, Madrid, Spain aut Muñoz-Montaño J. Centro de Biología Molecular ‘Severo Ochoa', Universidad Autónoma de Madrid, 28049, Cantoblanco, Madrid, Spain aut Avila Jesús Centro de Biología Molecular ‘Severo Ochoa', Universidad Autónoma de Madrid, 28049, Cantoblanco, Madrid, Spain aut Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 165/1(1996-12-01), 47-54 0300-8177 165:1<47 1996 165 11010 https://doi.org/10.1007/BF00229744 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00229744 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Moreno Francisco Centro de Biología Molecular ‘Severo Ochoa', Universidad Autónoma de Madrid, 28049, Cantoblanco, Madrid, Spain aut NATIONALLICENCE 700 1- Muñoz-Montaño J. Centro de Biología Molecular ‘Severo Ochoa', Universidad Autónoma de Madrid, 28049, Cantoblanco, Madrid, Spain aut NATIONALLICENCE 700 1- Avila Jesús Centro de Biología Molecular ‘Severo Ochoa', Universidad Autónoma de Madrid, 28049, Cantoblanco, Madrid, Spain aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 165/1(1996-12-01), 47-54 0300-8177 165:1<47 1996 165 11010 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer