p-21-activated kinase 6 (PAK6) is a serine-threonine protein kinase originally identified as an Androgen Receptor (AR) interacting protein. In current study, we determined the subcellular localization of PAK6 through mutational analysis. We have found that the N-terminal CRIB domain is partly responsible for plasma membrane targeting, the region between amino acid residues #292 to #368 is functionally relevant to plasma membrane localization and that amino acid residues #119 through #190 are responsible for nuclear targeting of PAK6, in addition to a stretch of positively charged N-terminal residues (#2-#11) since mutants lacking this sequence mis-localizes to cytoplasm. In junction forming epithelial cells, PAK6 is demonstrated to co-localize with B-catenin at adherens junctions, suggesting that PAK6 is an activation-dependent event and that PAK6 translocates from plasma membrane to the cytoplasm in response activation via the PKA signal pathway. / by Ciny John. / Thesis (M.S.)--Florida Atlantic University, 2012. / Includes bibliography. / Mode of access: World Wide Web. / System requirements: Adobe Reader.
Identifer | oai:union.ndltd.org:fau.edu/oai:fau.digital.flvc.org:fau_3940 |
Contributors | John, Ciny, Charles E. Schmidt College of Medicine, Department of Biomedical Science |
Publisher | Florida Atlantic University |
Source Sets | Florida Atlantic University |
Language | English |
Detected Language | English |
Type | Text, Electronic Thesis or Dissertation |
Format | viii, 48 p. : ill. (some col.), electronic |
Rights | http://rightsstatements.org/vocab/InC/1.0/ |
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