Event Website
http://www.bates.edu/mt-david-summit.xml
Start Date
1-4-2011 1:45 PM
End Date
1-4-2011 3:00 PM
Description
Protein kinases have been implicated in mediating prometastatic signaling in human cancers. RSK2 is a member of the family of 90-kDa ribosomal S6 kinases. The RSK2 pathway is a key regulator of cancer proliferation. Serine/threonine kinases play a key role in the mitogen activated protein (MAP) kinase signaling pathway, which is important in cell proliferation and oncogenesis. RSK2 is activated in response to a number of different stimuli such as insulin, growth factors, neurotransmitters, and chemokines (Sturgill et al. 1988), and upon activation RSK2 moves from the cell cytoplasm into the nucleus. There, RSK2 phosphorylates a wide range of nuclear substrates such as transcription factors. This RSK2 activity contributes to cell division, and when cells divide over and over again it leads to cancer and tumor formation. Research has been done to see how RSK2 localizes into the nucleus; however, the mechanism is still not understood. As a way to better our understanding of the mechanism in which RSK2 localizes in the nucleus, I have mutated RSK2 to determine which amino acid residue is key in localizing RSK2 into the nucleus. This could eventually lead to the development of more treatment options for certain cancers such as breast cancer and head and neck squamous cell cancer (HNSCC).
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Mutagenesis of RSK2 to Locate Nuclear Localization Signal of RSK2
Protein kinases have been implicated in mediating prometastatic signaling in human cancers. RSK2 is a member of the family of 90-kDa ribosomal S6 kinases. The RSK2 pathway is a key regulator of cancer proliferation. Serine/threonine kinases play a key role in the mitogen activated protein (MAP) kinase signaling pathway, which is important in cell proliferation and oncogenesis. RSK2 is activated in response to a number of different stimuli such as insulin, growth factors, neurotransmitters, and chemokines (Sturgill et al. 1988), and upon activation RSK2 moves from the cell cytoplasm into the nucleus. There, RSK2 phosphorylates a wide range of nuclear substrates such as transcription factors. This RSK2 activity contributes to cell division, and when cells divide over and over again it leads to cancer and tumor formation. Research has been done to see how RSK2 localizes into the nucleus; however, the mechanism is still not understood. As a way to better our understanding of the mechanism in which RSK2 localizes in the nucleus, I have mutated RSK2 to determine which amino acid residue is key in localizing RSK2 into the nucleus. This could eventually lead to the development of more treatment options for certain cancers such as breast cancer and head and neck squamous cell cancer (HNSCC).
http://scarab.bates.edu/mt_david_summit/MDS2011/02Poster/1