| Texto completo | |
| Autor(es): Mostrar menos - |
Duarte, Mariana Lemos
;
Pena, Darlene Aparecida
;
Nunes Ferraz, Felipe Augusto
;
Berti, Denise Aparecida
;
Paschoal Sobreira, Tiago Jose
;
Costa-Junior, Helio Miranda
;
Abdel Baqui, Munira Muhammad
;
Disatnik, Marie-Helene
;
Xavier-Neto, Jose
;
Lopes de Oliveira, Paulo Sergio
;
Schechtman, Deborah
Número total de Autores: 11
|
| Tipo de documento: | Artigo Científico |
| Fonte: | SCIENCE SIGNALING; v. 7, n. 350, p. 8-pg., 2014-11-04. |
| Resumo | |
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) | |
| Processo FAPESP: | 11/10321-3 - Caracterização funcional da proteína cinase c beta 1 na auto-renovação |
| Beneficiário: | Darlene Aparecida Pena |
| Modalidade de apoio: | Bolsas no Brasil - Doutorado |
| Processo FAPESP: | 12/24154-4 - Anticorpos conformacionais específicos para a PKC beta I e suas aplicações |
| Beneficiário: | Deborah Schechtman |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| Processo FAPESP: | 10/18640-8 - PKC e vias de sinalização da auto-renovação e diferenciação de células tronco embrionárias murinas |
| Beneficiário: | Deborah Schechtman |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| Processo FAPESP: | 06/52062-6 - Caracterização das diferentes isoenzimas das proteínas cinases C e seus substratos em células tronco embrionárias murinas não diferenciadas |
| Beneficiário: | Helio Miranda Costa Junior |
| Modalidade de apoio: | Bolsas no Brasil - Pós-Doutorado |
| Processo FAPESP: | 10/15424-2 - Mecanismos de Translocação Nuclear da Proteína Quinase C BI nas Células Tronco Embrionárias Murinas |
| Beneficiário: | Denise Aparecida Berti |
| Modalidade de apoio: | Bolsas no Brasil - Pós-Doutorado |