Current Search:  Phosphorylation (x)

View All Items

  • CSV Spreadsheet
(1 - 3 of 3)
Control of Mitochondrial αB-crystallin Function by Phosphorylation
Title
Control of Mitochondrial αB-crystallin Function by Phosphorylation.
Creator
Posada, Angie, Kantorow, Marc, Florida Atlantic University, Charles E. Schmidt College of Medicine, Department of Biomedical Science
Abstract/Description
αB-crystallin is a small heat-shock chaperone protein (sHSP) required for the homeostasis of multiple tissues including eye lens, retina, heart and brain. Correspondingly, mutation or altered levels of αB-crystallin are associated with multiple degenerative diseases including cataract, retinal degeneration, cardiomyopathy and Lewy body disease. Based on its wide-ranging importance understanding the protective and homeostatic properties of α B-crystallin is critical for understanding...
Show moreαB-crystallin is a small heat-shock chaperone protein (sHSP) required for the homeostasis of multiple tissues including eye lens, retina, heart and brain. Correspondingly, mutation or altered levels of αB-crystallin are associated with multiple degenerative diseases including cataract, retinal degeneration, cardiomyopathy and Lewy body disease. Based on its wide-ranging importance understanding the protective and homeostatic properties of α B-crystallin is critical for understanding degenerative diseases and could lead to the development of therapies to treat these diseases. αB-crystallin is localized to the mitochondria suggesting a direct effect on mitochondrial function. My thesis work has examined those molecular pathways required for translocation of αB-crystallin to the mitochondria and to identify the downstream pathways controlled by mitochondrial translocation of αB-crystallin that could be important for cellular protection and differentiation. My results point to a novel role of αB-crystallin in regulation of key apoptotic pathways that mediate the balance between cell survival and differentiation.
Show less
Date Issued
2018
PURL
http://purl.flvc.org/fau/fd/FA00013166
Subject Headings
alpha-Crystallin B Chain, Mitochondria, Phosphorylation, Degenerative diseases
Format
Document (PDF)
REGULATION OF CASPASE-3 ACTIVATION BY PHOSPHORYALTED Ab-CRYSTALLIN AND ITS ROLE IN DIFFERENTIATION
Title
REGULATION OF CASPASE-3 ACTIVATION BY PHOSPHORYALTED Ab-CRYSTALLIN AND ITS ROLE IN DIFFERENTIATION.
Creator
Cherubin, Patrice, Kantorow, Marc, Florida Atlantic University, Charles E. Schmidt College of Medicine, Department of Biomedical Science
Abstract/Description
The lens is responsible for focusing light into the retina. It accomplishes this through its maturation from an epithelial cell into a fiber cell. A large amount of research has been done on cellular differentiation. Nevertheless, we still lack knowledge on many different aspects of differentiation, including a complete theory on the mechanism behind differentiation. Due to the lens’ unique structure and cell types, this is an ideal model for studying differentiation. Our research has shown...
Show moreThe lens is responsible for focusing light into the retina. It accomplishes this through its maturation from an epithelial cell into a fiber cell. A large amount of research has been done on cellular differentiation. Nevertheless, we still lack knowledge on many different aspects of differentiation, including a complete theory on the mechanism behind differentiation. Due to the lens’ unique structure and cell types, this is an ideal model for studying differentiation. Our research has shown that αB crystallin, a small heat shock protein, is able to modulate cytochrome C levels and protect the mitochondria under oxidative stress. Also, cytochrome C release is often followed by caspase 3 activation. In addition, research has shown that low levels of caspase 3 activation is essential in driving differentiation. My work examined if αB crystallin could modulate cytochrome C to lower caspase 3 levels to allow for differentiation rather than apoptosis.
Show less
Date Issued
2019
PURL
http://purl.flvc.org/fau/fd/FA00013293
Subject Headings
Caspase 3, Cell differentiation, Crystallins, Phosphorylation, Cytochromes C
Format
Document (PDF)
Determining the subcellular localization of a group II p21-activated kinase - PAK6
Title
Determining the subcellular localization of a group II p21-activated kinase - PAK6.
Creator
John, Ciny, Charles E. Schmidt College of Medicine, Department of Biomedical Science
Abstract/Description
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...
Show morep-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.
Show less
Date Issued
2012
PURL
http://purl.flvc.org/FAU/3355569
Subject Headings
Cellular signal transduction, Serine proteinases, Phosphorylation, Protein kinases, Pathophysiology, Phosphoroproteins, Metabolism
Format
Document (PDF)