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The role of the DEK1 pathway in plant epidermis cell fate specification (Plant epidermis)
Start date: Jan 1, 2010, End date: Dec 31, 2013 PROJECT  FINISHED 

This proposal has three major strands to it: (i) The return of Prof Olsen from seven years of work experience in two of the major US plant Biotech companies (Pioneer Hi-Bred International, a DuPont Company and the Monsanto Company) to head up a research project and further develop strategic plans for plant research at the Norwegian University for Biosciences and Hamar University College, (ii) a specific research project, to be centered at UMB, but which will also involve the development of collaborations with Hedmark University College in Norway as well as five USA industrial and academic partners, (iii) the future development of European collaborative research projects within the KBBE program. Research program - Epidermal cell fate specification and maintenance in plants are widely recognized to occur via positional signaling, including maize aleurone cells that form exclusively in response to surface position. Three maize proteins have been implicated in position-dependant aleurone cell formation, e.i. DEK1, a membrane anchored calpain-like proteinase, CR4, a receptor kinase and SAL1, a class E vacuolar sorting protein. Recent data has suggested a model for aleurone cell fate specification in which DEK1 perceives and/or transmits a positional signal via the external loop region activating its calpain proteinase , CR4 promotes lateral movement of aleurone signaling molecules between aleurone cells in specialized aleurone cell plasmodesmata, and SAL1 maintains the proper plasma membrane concentration of DEK1 and CR4 proteins via endosome mediated recycling/degradation. Data from Arabidopsis and other plants implicate these three genes in epidermal cell fate specification in all plants and all plant organs. This project aims at (I) identifying the domain(s) of the DEK1 protein that perceives cell surface position, (II) identifying the proposed positional ligand that activates DEK1 and (III) identifying the DEK1 substrate.
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