J Integr Plant Biol. ›› 2013, Vol. 55 ›› Issue (1): 7-20.DOI: 10.1111/jipb.12010

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Emerging Role of the Ubiquitin Proteasome System in the Control of Shoot Apical Meristem Function

Elisabetta Di Giacomo1, Giovanna Serino2,3 and Giovanna Frugis1*   

  1. 1Istituto di Biologia e Biotecnologia Agraria, UOS Roma, Consiglio Nazionale delle Ricerche, Via Salaria Km. 29,300-00015, Monterotondo Scalo, Roma, Italy
    2Dipartimento di Biologia e Biotecnologie Charles Darwin, Sapienza Università di Piazzale Aldo Moro 5, 00185 Roma, Italy
    3The New York Botanical Garden, Genomics Program NYBG, 2900 Southern Blvd. Bronx, NY 10458-5126, USA
  • Received:2012-10-08 Accepted:2012-11-02 Published:2013-01-01
  • About author:*Corresponding author Tel: +39 06 9067 2857; Fax: +39 06 9067 2856; E-mail: giovanna.frugis@ibba.cnr.it


The shoot apical meristem (SAM) is a population of undifferentiated cells at the tip of the shoot axis that establishes early during plant embryogenesis and gives rise to all shoot organs throughout the plant's life. A plethora of different families of transcription factors (TFs) play a key role in establishing the equilibrium between cell differentiation and stem cell maintenance in the SAM. Fine tuning of these regulatory proteins is crucial for a proper and fast SAM response to environmental and hormonal cues, and for development progression. One effective way to rapidly inactivate TFs involves regulated proteolysis by the ubiquitin/26S proteasome system (UPS). However, a possible role of UPS-dependent protein degradation in the regulation of key SAM TFs has not been thoroughly investigated. Here, we summarize recent evidence supporting a role for the UPS in SAM maintenance and function. We integrate this survey with an in silico analysis of publicly-available microarray databases which identified ubiquitin ligases that are expressed in specific areas within the SAM, suggesting that they may regulate or act downstream of meristem-specific factors.

Key words: Arabidopsis thaliana, UPS, cell differentiation, protein degradation, shoot apical meristem

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