Original title: Molekulární charakterizace interakcí γ -tubulinu se signálními molekulami
Translated title: Molecular characterization of γ -tubulin interactions with signalling molecules
Authors: Macůrek, Libor ; Dráber, Pavel (advisor) ; Binarová, Pavla (referee) ; Svoboda, Augustin (referee)
Document type: Doctoral theses
Year: 2007
Language: eng
Abstract: 52 V. CONCLUSIONS The results of presented PhD thesis can be summarized as follows: For the first time it has been demonstrated that γ-tubulin forms complexes with αβ-tubulin dimers in brain tissue as well as in other models of neuronal differentiation. Two forms of γ- tubulin have been identified in complexes of various sizes. It has been shown that γ-tubulin is posttranslationally modified. One of the identified posttranslational modifications of γ-tubulin is phosphorylation that appears to depend on Src family kinase activity. It has been proposed that posttranslational modifications of γ-tubulin may regulate interactions of γ-tubulin with αβ-tubulin heterodimers or other associated proteins during neurogenesis. It has been shown that γ-tubulin associates with protein tyrosine kinases involved in signal transduction events. γ-Tubulin interaction with Src family kinases significantly increased after long-term RA-activation embryonal carcinoma P19 cells. A similar increase has been observed after rapid activation of mast cells, indicating that this regulatory mechanism is not restricted to a particular model system. In both models, Src family kinases bound to γ-tubulin are active and phosphorylate proteins present in γ-tubulin complexes. Fyn kinase interacts with γ-tubulin through its SH2 domain in a...

Institution: Charles University Faculties (theses) (web)
Document availability information: Available in the Charles University Digital Repository.
Original record: http://hdl.handle.net/20.500.11956/95155

Permalink: http://www.nusl.cz/ntk/nusl-373564


The record appears in these collections:
Universities and colleges > Public universities > Charles University > Charles University Faculties (theses)
Academic theses (ETDs) > Doctoral theses