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Details

Autor(en) / Beteiligte
Titel
The E3 ubiquitin ligase WVIP2 highlights the versatility of protein ubiquitination
Ist Teil von
  • Plant signaling & behavior, 2012-09, Vol.7 (9), p.1155-1157
Ort / Verlag
United States: Informa UK Limited
Erscheinungsjahr
2012
Link zum Volltext
Quelle
Taylor & Francis Current Content Access
Beschreibungen/Notizen
  • Plant cells regulate many cellular processes controlling the half-life of critical proteins through ubiquitination. Previously, we characterized two interacting RING-type E3 ubiquitin ligases of Triticum durum, TdRF1 and WVIP2. We revealed their role in tolerance to dehydration, and existing knowledge about their partners also indicated their involvement in the regulation of some aspects of plant development. Here we located WVIP2 in the regulation of the ABA signaling, based on sequence similarities. Further we acquired general evidence about the versatility of ubiquitination in plant cells. A protein can be target of different E3 ligases for a perfect tuning of its abundance as well as the same E3 ligase can ubiquitinate different and unrelated proteins, thus representing a cross-connections between different signaling pathways for a global coordination of cellular processes.

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