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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Protein folding creates structure-based, noncontiguous consensus phosphorylation motifs recognized by kinases

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Author(s):
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Duarte, Mariana Lemos [1] ; Pena, Darlene Aparecida [1] ; Nunes Ferraz, Felipe Augusto [2] ; Berti, Denise Aparecida [1] ; Paschoal Sobreira, Tiago Jose [2] ; Costa-Junior, Helio Miranda [1] ; Abdel Baqui, Munira Muhammad [3] ; Disatnik, Marie-Helene [4] ; Xavier-Neto, Jose [2] ; Lopes de Oliveira, Paulo Sergio [2] ; Schechtman, Deborah [1]
Total Authors: 11
Affiliation:
[1] Univ Sao Paulo, Inst Quim, Dept Bioquim, BR-05508000 Sao Paulo - Brazil
[2] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Biociencias, BR-13083970 Campinas, SP - Brazil
[3] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Biol Celular & Mol, BR-14049900 Ribeirao Preto, SP - Brazil
[4] Stanford Univ, Sch Med, Dept Chem & Syst Biol, Stanford, CA 94305 - USA
Total Affiliations: 4
Document type: Journal article
Source: Science Signaling; v. 7, n. 350 NOV 4 2014.
Web of Science Citations: 20
Abstract

Linear consensus motifs are short contiguous sequences of residues within a protein that can form recognition modules for protein interaction or catalytic modification. Protein kinase specificity and the matching of kinases to substrates have been mostly defined by phosphorylation sites that occur in linear consensus motifs. However, phosphorylation can also occur within sequences that do not match known linear consensus motifs recognized by kinases and within flexible loops. We report the identification of Thr(253) in alpha-tubulin as a site that is phosphorylated by protein kinase C beta I (PKC beta I). Thr(253) is not part of a linear PKC consensus motif. Instead, Thr(253) occurs within a region on the surface of alpha-tubulin that resembles a PKC phosphorylation site consensus motif formed by basic residues in different parts of the protein, which come together in the folded protein to form the recognition motif for PKC beta I. Mutations of these basic residues decreased substrate phosphorylation, confirming the presence of this ``structurally formed{''} consensus motif and its importance for the protein kinase-substrate interaction. Analysis of previously reported protein kinase A (PKA) and PKC substrates identified sites within structurally formed consensus motifs in many substrates of these two kinase families. Thus, the concept of consensus phosphorylation site motif needs to be expanded to include sites within these structurally formed consensus motifs. (AU)

FAPESP's process: 11/10321-3 - Functional characterization of protein kinase c beta 1 in self-renewal
Grantee:Darlene Aparecida Pena
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 10/15424-2 - Mechanisms of nuclear translocation of protein kinase c bi in murine embryonic stem cells
Grantee:Denise Aparecida Berti
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 12/24154-4 - Specific conformational antibodies for PKC betaI and their aplications
Grantee:Deborah Schechtman
Support type: Regular Research Grants
FAPESP's process: 10/18640-8 - PKC and signal transduction pathways of self-renewal and differentiation in murine embryonic stem cells
Grantee:Deborah Schechtman
Support type: Regular Research Grants