J Cell Sci. CBMP Faculty. Development Accomplishing the specific aims in this proposal will establish the regulation of AJ dynamics as a key molecular and cellular mechanism by which Sdt, Crb and Lgl to control the apical-basal polarization in epithelial cells. Differential regulation of adherens junction dynamics during apical-basal polarization. To test this hypothesis, we have developed a novel genomic engineering approach in Drosophila that enables us to modify a target gene into any desired mutant alleles.
Yang Hong, Ph.D. Associate Professor Tel: Fax: Address: S BST-South [email protected] CBP Research Group(s). Yang Hong, Ph.D. Image - Yang Hong.
Title: Associate Professor Department: Dept of Cell Biology Email: [email protected] PubMed: Link Dept / Lab Webpage. Yang Hong of University of Pittsburgh, PA (Pitt) | Read 61 publications, and contact Yang Hong on ResearchGate, the professional network for scientists.
Establishing and maintaining apical-basal polarity is crucial for the function and structure of epithelia, while disruption of such polarity often accompanies the malignant transformation or stress-induced damage of epithelial cells.
Epub May 8. Lab Website. Yang Hong, Ph. Name University of Pittsburgh.
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|Cell Res. J Genet Genomics J Cell Biol J Cell Biol.
University of Pittsburgh Department of Cell Biology
Research in my lab focuses on the molecular mechanisms regulating the cell polarity.
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Regulation of Adherens Junction Trafficking by Polarity Proteins Yang Hong
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Here we propose that control of adherens junction AJ dynamics by polarity proteins Stardust SdtCrumbs Crb and Lethal giant larvae Lgl is an essential cellular mechanism for establishing apical-basal polarity. Accomplishing the specific aims in this proposal will establish the regulation of AJ dynamics as a key molecular and cellular mechanism by which Sdt, Crb and Lgl to control the apical-basal polarization in epithelial cells.
The ongoing projects focus on: 1 Mechanisms regulating the polarized membrane targeting of polarity proteins : Direct binding between Lgl and plasma membrane would localize Lgl to both apical and basolateral membrane domain, rather than exclusively to the basolateral domains.