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National Repository of Grey Literature 2 records found  Search took 0.01 seconds. 
Crosstalk of PKN3 and p130Cas/BCAR1 signaling
 Dibus, Michal ; Rösel, Daniel (advisor) ; Voller, Jiří (referee)
Both p130Cas and PKN3 are important regulators of cellular signaling deregulation of which leads to malignant behavior of cancer cells. Recently we have found that SH3 domain of p130Cas mediates interaction with proline rich region of PKN3 suggesting their possible cooperation in regulation of these processes. In this work we have focused on the phosphorylation of p130Cas by PKN3 and identified serine 498 (S498) within the serine rich domain of p130Cas to be phosphorylated by PKN3 in vitro. Given that S498 is localized within the 14-3-3 binding motif and its phosphorylation is required for interaction of p130Cas with 14-3-3 proteins, we propose potential existence of novel PKN3/p130Cas/14-3-3 signaling axis. In the second part of the work we have studied this pathway in response to antiestrogen treatment in estrogen receptor positive breast cancer cell line MCF7. Although we have shown inactivation of PKN3 occurs as an early response to tamoxifen treatment, we do not rule out its possible role in further promotion of resistance to antiestrogens. Furthermore, understanding the signaling triggered by interaction of PKN3 with p130Cas and its possible downstream effects on promoting malignant growth of cancer cells would help in finding novel therapeutic targets.
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A comparison of SH3 domains' tyrosine phosporylation influence on their binding capacity
 Tatárová, Zuzana ; Novotný, Marian (advisor) ; Kuthan, Martin (referee)
Understanding the impact of protein phosphorylation is very important for the formation of dynamic biological processes such as gene silencing, cell growth, differentiation or apoptosis. This work deals with the phosphorylation of a protein-interaction module known as SH3 domain and the influence of phosphorylation on its ligand-binding capacity. SH3 domain is a part of a large number of enzymes directly involved in signal transduction as well as adapter proteins without enzymatic activity. Many studies have shown the importance of tyrosine sites within SH3 domain in regulatory mechanisms of proteins by using either mutants that cannot be phosphorylated, mutants mimicking the negative charges created by phosphorylation or by evidence of in vivo phosphorylation. The work also includes bioinformatic analysis, which further expand our knowledge of SH3 phosphorylated proteins and confirms that phosphorylation of the tyrosine sites is conserved among proteins containing the SH3 domain.
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