Presentation Title
An Investigation into a Retriever-mediated Recycling Pathway in Arabidopsis thaliana
Abstract
The ability to recycle plasma membrane proteins from endosomes gives plants ready access to a pool of synthesized proteins, providing for quick responses to an ever-changing environment. Recently, a novel member of the Vacuolar Protein Sorting 26 gene family (VPS26C) has been shown to be a member of a retriever complex required for the recycling of plasma membrane proteins in human cells and polarized growth and cell wall organization in Arabidopsis thaliana roots (McNally et al., 2017; Jha et al., 2018). The short root hair phenotype of vps26c can be complemented by GFP fusions to both the human and Arabidopsis VPS26C orthologs. Of the proteins demonstrated to interact with VPS26C in human cells, CCDC22 (At1G55830) and CCDC93 (At4G32560) have homologs in Arabidopsis. Both ccdc22 and ccdc93 in Arabidopsis display short root hair phenotypes similar to that of vps26c, potentially due to participation in a common recycling pathway. To probe the function of CCDC22 and CCDC93 in Arabidopsis and the possible conservation of a VPS26C recycling pathway between humans and Arabidopsis, complemented lines expressing RFP-fusions to CCDC22 and CCDC93 are being developed. These lines will be used to localize these proteins in cells and determine if they co-localize with GFP-VPS26C on endosomal membranes. To investigate if they are part of a larger protein complex, antibodies against RFP will be used in immunoprecipitation assays to identify interacting partners. Lastly, we will test the model that VPS26C participates in the recycling of proteins from endosomes to the plasma membrane in Arabidopsis seedling roots.
Primary Faculty Mentor Name
Mary Tierney
Faculty/Staff Collaborators
Mary Tierney
Status
Graduate
Student College
College of Agriculture and Life Sciences
Program/Major
Plant Biology
Primary Research Category
Biological Sciences
An Investigation into a Retriever-mediated Recycling Pathway in Arabidopsis thaliana
The ability to recycle plasma membrane proteins from endosomes gives plants ready access to a pool of synthesized proteins, providing for quick responses to an ever-changing environment. Recently, a novel member of the Vacuolar Protein Sorting 26 gene family (VPS26C) has been shown to be a member of a retriever complex required for the recycling of plasma membrane proteins in human cells and polarized growth and cell wall organization in Arabidopsis thaliana roots (McNally et al., 2017; Jha et al., 2018). The short root hair phenotype of vps26c can be complemented by GFP fusions to both the human and Arabidopsis VPS26C orthologs. Of the proteins demonstrated to interact with VPS26C in human cells, CCDC22 (At1G55830) and CCDC93 (At4G32560) have homologs in Arabidopsis. Both ccdc22 and ccdc93 in Arabidopsis display short root hair phenotypes similar to that of vps26c, potentially due to participation in a common recycling pathway. To probe the function of CCDC22 and CCDC93 in Arabidopsis and the possible conservation of a VPS26C recycling pathway between humans and Arabidopsis, complemented lines expressing RFP-fusions to CCDC22 and CCDC93 are being developed. These lines will be used to localize these proteins in cells and determine if they co-localize with GFP-VPS26C on endosomal membranes. To investigate if they are part of a larger protein complex, antibodies against RFP will be used in immunoprecipitation assays to identify interacting partners. Lastly, we will test the model that VPS26C participates in the recycling of proteins from endosomes to the plasma membrane in Arabidopsis seedling roots.