Event Title

Session 2K: Identifying key functions of EphA1 and EphA2 in the epidermis

Session Number

Session 2K: 1st Presentation

Advisor(s)

Professor Bethany E. Perez-White and Nihal Kaplan, and Rosa Ventrella, Northwestern University

Location

Room A133

Start Date

26-4-2018 10:35 AM

End Date

26-4-2018 11:20 AM

Abstract

Ephrin type A receptor 1 (EphA1) and Ephrin type A receptor 2 (EphA2) are highly related receptor tyrosine kinases that play a role in skin function. We have previously reported that loss of EphA2 severely impairs epidermal differentiation. However, despite high homology, EphA1 cannot restore the

differentiation defect caused by lack of EphA2 suggesting that they have non-redundant functions in skin. Therefore, we hypothesize that EphA1 and EphA2 orchestrate distinct signaling networks in epidermis. To test this hypothesis, we used biotin-identification proteomics to identify proteins associated with EphA1 and/or EphA2.We identified 99 proteins that potentially associated with EphA1 and 196 with EphA2. Bioinformatic analysis using the Kyoto Encyclopedia of Genes and Genomes uncovered differences in the pathways associated with our proteomic interactome datasets for EphA1 and EphA2. Adherens junctions-associated proteins were prominent for EphA1 interacting proteins (FDR = 3.96e-09 ). While in the EphA2 dataset, endocytosis was seen emerged as the highest represented pathway (FDR = 9.46e-03). This data imply that EphA1 and EphA2 participate in distinct signaling pathways in epidermis.

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Apr 26th, 10:35 AM Apr 26th, 11:20 AM

Session 2K: Identifying key functions of EphA1 and EphA2 in the epidermis

Room A133

Ephrin type A receptor 1 (EphA1) and Ephrin type A receptor 2 (EphA2) are highly related receptor tyrosine kinases that play a role in skin function. We have previously reported that loss of EphA2 severely impairs epidermal differentiation. However, despite high homology, EphA1 cannot restore the

differentiation defect caused by lack of EphA2 suggesting that they have non-redundant functions in skin. Therefore, we hypothesize that EphA1 and EphA2 orchestrate distinct signaling networks in epidermis. To test this hypothesis, we used biotin-identification proteomics to identify proteins associated with EphA1 and/or EphA2.We identified 99 proteins that potentially associated with EphA1 and 196 with EphA2. Bioinformatic analysis using the Kyoto Encyclopedia of Genes and Genomes uncovered differences in the pathways associated with our proteomic interactome datasets for EphA1 and EphA2. Adherens junctions-associated proteins were prominent for EphA1 interacting proteins (FDR = 3.96e-09 ). While in the EphA2 dataset, endocytosis was seen emerged as the highest represented pathway (FDR = 9.46e-03). This data imply that EphA1 and EphA2 participate in distinct signaling pathways in epidermis.