Kafatos:Povelones, Michael: Difference between revisions
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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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* [[pmid:18497855 |Habtewold T, Povelones M, Blagborough AM, Christophides GK. Transmission Blocking Immunity in the Malaria Non-Vector Mosquito ''Anopheles quadriannulatus'' Species A. PLoS Pathog. 2008 May 23;4(5).]] | |||
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===Previous Research=== | ===Previous Research=== | ||
<font size="3">I received my doctoral degree at [http://www.stanford.edu Stanford University] in the laboratory of [http://www.stanford.edu/~rnusse/ 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 [http://www.stanford.edu Stanford University] in the laboratory of [http://www.stanford.edu/~rnusse/ 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> |
Revision as of 13:12, 26 May 2008
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Michael Povelones
Division of Cell & Molecular Biology
Imperial College |
Education
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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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