Determine the Mechanism by Which specific ErbB Receptor Dimers Differ in Their Ability to Disrupt Epithelial Cell Polarity
Abstract
Loss is epithelial architecture is thought to be an early event in carcinoma. The mechanism by which oncogenes disrupt epithelial architecture is poorly underst?od. Preyious results froin our lab have shown that ErbB2, an oncogene correlated to poor clinical prognosis in breast-cancer, can disrupt epithelial cell polarity. My research is aimed at investigating how activation of ErbB2 disrupts epithelial cell polarity-. - Activation of ErbB2 is known to induce phophorylation of five tyrosines in its cytoplasmic tail. Using ErbB2 autophosphorylation site mutants, I investigated whether a particular tyrosine residue mediates the ErbB2-induced changes in epithelial cell polarity. In my first series of studies, where one of the five tyrosines was mutated to phenylalanine, I have identified that loss of-Tyr 1144 inactivates the ability of ErbB2 to disrupt cell polarity suggesting that Tyr1144 is required for ErbB2-induced changes in polarity. I am in the process of completing my analyses to investigate whether Tyr 1144 or other tyrosine is sufficient to mediate ErbB2-induced changes in polarity and identify the tyrosine -residues that mediate-the ErbB2-induced changes in the Par' protein complex.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 01, 2005
- Accession Number
- ADA437188
Entities
People
- Alexandra V. Lucs
Organizations
- Cold Spring Harbor Laboratory