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Title page for ETD etd-07192012-173715

Type of Document Dissertation
Author Markham, Nicholas Owen
URN etd-07192012-173715
Title DIPA is a novel, isoform-specific binding partner of the tumor-associated p120 isoform 1
Degree PhD
Department Cancer Biology
Advisory Committee
Advisor Name Title
Robert J. Coffey Committee Chair
Albert B. Reynolds Committee Member
Christopher S. Williams Committee Member
David Cortez Committee Member
Scott W. Hiebert Committee Member
  • adherens junctions
  • DIPA
  • p120-catenin
Date of Defense 2012-06-18
Availability unrestricted
p120-catenin (p120) is a master regulator of cellular adherens junctions and is important for epithelial homeostasis, development, tumorigenesis, and metastasis. Relatively little is known about the different functions of p120 isoforms. During validation of a yeast two-hybrid screen using p120 as bait, I detected an isoform-specific interaction with Delta-Interacting Protein A (DIPA). In this study, I show that DIPA co-localizes and co-immunoprecipitates reciprocally with the long p120-1 isoform, but not the shorter p120-3 isoform, which lacks an N-terminal head domain. Also, p120-1 expression is required for the plasma membrane localization of DIPA. The p120 family members ARVCF, p0071, and δ-catenin have similar N-terminal regions to p120-1 and also bind to DIPA, suggesting that the interaction is highly conserved. These family members can recruit DIPA to the plasma membrane in the absence of p120-1. DIPA is the first protein discovered to selectively interact with isoform p120-1, and my data suggest that their relationship is potentially important for a novel, cell contact mediated function.
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