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Descripción
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| POSTER: Coordination between cell division and cell differentiation is crucial for growth and development of eukaryotic organisms. Progression through the different phases of cell division requires the specific degradation of proteins through the ubiquitin-proteasome 26S pathway (Ub/26S). In plants, this pathway plays a key role in controlling several developmental processes and responses, including cell proliferation. Ubiquitin is attached to target proteins in sequential biochemical cascade that involves the E1,E2 and E3 enzymes. There are different types of E3. Oneof these types is the SCF complex, which is composed of 4 protein subunits, CUL1, RBX, ASK1 and an F-box. SKP2A is an F-box protein forms an SCF complex in vivo that has E3 ubiquitin ligase activity. SKP2A regulates the stability of the cell division E2FC-DPB repressor transcription factor, and subsequently positively regulates cell division. Plants that over-express SKP2A increase the number of cells in G2/M, reduce the level of ploidy and develop higher number of lateral root primordia. Interestingly, SKP2A is degraded through the Ub/26S pathway and auxin regulates such degradation. We have found that auxin is capable of regulating SKP2A stability in a cell free system, suggesting that the regulation of auxin is direct. Taken together, our results indicate that SKP2A is a positive regulator of cell division and its stability is controlled by auxin-dependent degradation. | |
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Internacional
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Si |
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Nombre congreso
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20TH International Conference on Arabidopsis Research |
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Tipo de participación
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960 |
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Lugar del congreso
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Revisores
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Si |
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ISBN o ISSN
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0000-0000 |
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DOI
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Fecha inicio congreso
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30/06/2009 |
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Fecha fin congreso
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04/07/2009 |
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Desde la página
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45 |
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Hasta la página
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46 |
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Título de las actas
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LIBRO DE RESUMENES |