Molecular mechanisms underlying Maspin biological activities
Maspin - function and signaling pathways in the mouse mammary epithelium
Maspin in cell stress response and intercellular communication
Grant number: | 09/12597-6 |
Support Opportunities: | Scholarships in Brazil - Master |
Start date: | March 01, 2011 |
End date: | February 29, 2012 |
Field of knowledge: | Biological Sciences - Biochemistry - Molecular Biology |
Principal Investigator: | Nathalie Cella |
Grantee: | Mariana Tamazato Longhi |
Host Institution: | Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil |
Abstract Posttranslational modifications are critical for several protein functions, modulating protein activity, subcellular localization and dynamic interactions with other proteins. Our group is exploring the biological properties of maspin, a protein which belongs to the serpin family (serine protease inhibitor) due to sequence homology, albeit it does not inhibit proteases. A single gene has been described for maspin, but a great diversity of biological functions can be observed, including modulation of cell adhesion, inhibition of growth and tumor invasion, inhibition of angiogenesis, pro-apoptotic effect and control of the oxidative stress response. This function diversity reflects the great number of ligands described for maspin and its subcellular localization, since it can be found in the nucleus, cytoplasm and cell membrane. Since the vast diversity of biological functions and locations of a protein cannot be explained only by its primary structure, posttranslational modification such as phosphorylation, acetylation, methylation, ubiquitination and sumoylation are likely to be involved. Accordingly, the objective of this proposal is to characterize possible posttranslational modifications on maspin, particularly phosphorylation and sumoylation, and correlate them to its subcellular localization. | |
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