Kafatos:Povelones, Michael: Difference between revisions
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=Education= | ===Education=== | ||
<font size="3">BA in Chemistry, Columbia University, New York, NY, USA<br> | <font size="3">BA in Chemistry, Columbia University, New York, NY, USA<br> | ||
PhD in Developmental Biology, Stanford University, Stanford, CA, USA<br> | PhD in Developmental Biology, Stanford University, Stanford, CA, USA<br> | ||
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=Current Research Interests= | ===Current Research Interests=== | ||
<font size="3">I am a postdoctoral fellow in the [[kafatos:Kafatos/Christophides Lab|Kafatos/Christophides Lab]] at [http://www.imperial.ac.uk/ Imperial College], London. Science is cool.</font> | <font size="3">I am a postdoctoral fellow in the [[kafatos:Kafatos/Christophides Lab|Kafatos/Christophides Lab]] at [http://www.imperial.ac.uk/ Imperial College], London. Science is cool.</font> | ||
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===Previous Research=== | |||
<font size="3">I received my doctoral degree at Stanford University in the laboratory of Roel Nusse. The focus of my research was understanding how the ''frizzled (fz)'' receptor in ''Drosophila'' functions in planar cell polarization (PCP) and Wnt-mediated cell fate specification. ''fz'' controls two different signal transduction pathways for each of these distinct developmental outcomes. How does a single receptor function in two signaling pathways? This work revealed that even though cell fate signaling requires a Wnt ligand, ''fz'' is not activated by any of the 7 ''Drosophila'' Wnt genes for its PCP function. Instead, ''fz'' has an intrinsic ability to control components of the PCP pathway and that it associates with pathway specific Wnt co-receptor for cell fate signaling. In addition, a structure-function analysis of ''fz'' suggested that, in addition to the Wnt binding site located in the extracellular cysteine-rich domain, there is a second Wnt-binding site within the transmembrane portion of the receptor.</font> | <font size="3">I received my doctoral degree at Stanford University in the laboratory of Roel Nusse. The focus of my research was understanding how the ''frizzled (fz)'' receptor in ''Drosophila'' functions in planar cell polarization (PCP) and Wnt-mediated cell fate specification. ''fz'' controls two different signal transduction pathways for each of these distinct developmental outcomes. How does a single receptor function in two signaling pathways? This work revealed that even though cell fate signaling requires a Wnt ligand, ''fz'' is not activated by any of the 7 ''Drosophila'' Wnt genes for its PCP function. Instead, ''fz'' has an intrinsic ability to control components of the PCP pathway and that it associates with pathway specific Wnt co-receptor for cell fate signaling. In addition, a structure-function analysis of ''fz'' suggested that, in addition to the Wnt binding site located in the extracellular cysteine-rich domain, there is a second Wnt-binding site within the transmembrane portion of the receptor.</font> | ||
[[Image:Kafatos-pove-fz.png|right|220px]] | [[Image:Kafatos-pove-fz.png|right|220px]] |
Revision as of 13:55, 19 August 2006
Michael Povelones Division of Cell & Molecular Biology |
EducationBA in Chemistry, Columbia University, New York, NY, USA |
Current Research InterestsI am a postdoctoral fellow in the Kafatos/Christophides Lab at Imperial College, London. Science is cool. |
Previous ResearchI received my doctoral degree at Stanford University in the laboratory of Roel Nusse. The focus of my research was understanding how the frizzled (fz) receptor in Drosophila functions in planar cell polarization (PCP) and Wnt-mediated cell fate specification. fz controls two different signal transduction pathways for each of these distinct developmental outcomes. How does a single receptor function in two signaling pathways? This work revealed that even though cell fate signaling requires a Wnt ligand, fz is not activated by any of the 7 Drosophila Wnt genes for its PCP function. Instead, fz has an intrinsic ability to control components of the PCP pathway and that it associates with pathway specific Wnt co-receptor for cell fate signaling. In addition, a structure-function analysis of fz suggested that, in addition to the Wnt binding site located in the extracellular cysteine-rich domain, there is a second Wnt-binding site within the transmembrane portion of the receptor.
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