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Determining the subcellular localization of a group II p21-activated kinase - PAK6
- Date Issued:
- 2012
- Summary:
- 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.
Title: | Determining the subcellular localization of a group II p21-activated kinase - PAK6. |
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Name(s): |
John, Ciny Charles E. Schmidt College of Medicine Department of Biomedical Science |
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Type of Resource: | text | |
Genre: | Electronic Thesis Or Dissertation | |
Date Issued: | 2012 | |
Publisher: | Florida Atlantic University | |
Physical Form: | electronic | |
Extent: | viii, 48 p. : ill. (some col.) | |
Language(s): | English | |
Summary: | 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. | |
Identifier: | 820353539 (oclc), 3355569 (digitool), FADT3355569 (IID), fau:3940 (fedora) | |
Note(s): |
by Ciny John. Thesis (M.S.)--Florida Atlantic University, 2012. Includes bibliography. Mode of access: World Wide Web. System requirements: Adobe Reader. |
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Subject(s): |
Cellular signal transduction Serine proteinases Phosphorylation Protein kinases -- Pathophysiology Phosphoroproteins -- Metabolism |
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Persistent Link to This Record: | http://purl.flvc.org/FAU/3355569 | |
Use and Reproduction: | http://rightsstatements.org/vocab/InC/1.0/ | |
Host Institution: | FAU |