Kia Perez-Vale

 

KiaLabPic
Background & Contact Information

Position Graduate Student (2016-Present)
Education: BS, University of Puerto Rico-Arecibo 2014; UNC PREP 2014-2015
Fellowships & Awards: NIH T32 Training Program in Genetics and Molecular Biology
Email: kiaperez@unc.edu
DOWNLOAD CV

 

KiaScience_Photo

Research Information

During embryonic development, adult homeostasis, and wound healing, cells need to change shape and move while maintaining tissue integrity. Cell-cell adherens junctions (AJs) are essential for cell adhesion and cell shape changes. They also serve as key polarity landmarks, defining the boundary between apical and basolateral domains. Loss of cell-cell junctions and polarity are crucial for cancer metastasis. Thus, it is critical to understand the mechanism of action of junctional and polarity proteins, which allow them to accomplish these roles.

 

An outstanding model to study apical-basal polarity establishment is the cellularizing Drosophila embryo. Canoe (Cno; homolog of human Afadin) regulates the polarized localization of Bazooka (Baz; homolog of human Par3), a key polarity protein that regulates polarization of the apical-basal axis, and positions proteins of the cell-cell AJ apically. Previous work from our lab revealed that Cno is a key polarity landmark, acting at the top of the current regulatory hierarchy by spatially restricting both Baz and the AJ protein beta-catenin. Our data suggest that Cno acts as an AJ-actin cytoskeleton linker, and we hypothesized it mediates correct Baz localization through its interactions with the polarised actin cytoskeleton. The first question that I set out to address is where within the cell Cno functions, and how it localizes there. Cno’s structure suggests a scaffolding role; we are particularly interested in the two N-terminal Ras association (RA) domains, for which the small GTPase Rap1 is the preferred binding partner, and the C-terminal actin-binding domain. Cno localizes to AJs in a Rap1 and actin-dependent manner. Rap1 is thought to activate Cno, but the mechanism by which it does so remains unclear. Our data suggests that Rap1 may act in a more indirect way to facilitate Cno localization. We are currently exploring other Rap1 partners that may mediate Cno localization. As well as identifying the guanine nucleotide exchange factor responsible for activating Rap1 at the AJs during cellularization. Together, these data will reveal the most upstream steps in polarity establishment.

Publications

Perez-Vale, K.Z., and Peifer, M.  (2018).  Modulating Apical-Basal Polarity by Building and Deconstructing a Yurt.  Journal of Cell Biology, in press.

Bonello, T.T., Perez-Vale, K.Z., Sumigray, K.D., and Peifer, M.  (2018)  Rap1 acts via multiple mechanisms to position Canoe/Afadin and adherens junctions and mediate apical-basal polarity establishment. .

Comments are closed.

Copyright 2019 Peifer Lab · RSS Feed · Log in

Site By: Ruby Red Design Studio

Mark Peifer Mark Peifer