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Displaying results 1 to 2 of 2.
Dong, H.; Dumenil, J.; Lu, F.-H.; Na, L.; Vanhaeren, H.; Naumann, C.; Klecker, M.; Prior, R.; Smith, C.; McKenzie, N.; Saalbach, G.; Chen, L.; Xia, T.; Gonzalez, N.; Seguela, M.; Inze, D.; Dissmeyer, N.; Li, Y.; Bevan, M. W.; Ubiquitylation activates a peptidase that promotes cleavage and destabilization of its activating E3 ligases and diverse growth regulatory proteins to limit cell proliferation in Arabidopsis Genes Dev. 31, 197-208, (2017) DOI: 10.1101/gad.292235.116
The characteristic shapes and sizes of organs are established by cell proliferation patterns and final cell sizes, but the underlying molecular mechanisms coordinating these are poorly understood. Here we characterize a ubiquitin-activated peptidase called DA1 that limits the duration of cell proliferation during organ growth in Arabidopsis thaliana. The peptidase is activated by two RING E3 ligases, Big Brother (BB) and DA2, which are subsequently cleaved by the activated peptidase and destabilized. In the case of BB, cleavage leads to destabilization by the RING E3 ligase PROTEOLYSIS 1 (PRT1) of the N-end rule pathway. DA1 peptidase activity also cleaves the deubiquitylase UBP15, which promotes cell proliferation, and the transcription factors TEOSINTE BRANCED 1/CYCLOIDEA/PCF 15 (TCP15) and TCP22, which promote cell proliferation and repress endoreduplication. We propose that DA1 peptidase activity regulates the duration of cell proliferation and the transition to endoreduplication and differentiation during organ formation in plants by coordinating the destabilization of regulatory proteins.
Dong, H.; Dumenil, J.; Lu, F.-H.; Na, L.; Vanhaeren, H.; Naumann, C.; Klecker, M.; Prior, R.; Smith, C.; McKenzie, N.; Saalbach, G.; Chen, L.; Xia, T.; Gonzalez, N.; Seguela, M.; Inze, D.; Dissmeyer, N.; Li, Y.; Bevan, M. W.; Ubiquitylation activates a peptidase that promotes cleavage and destabilization of its activating E3 ligases and diverse growth regulatory proteins to limit cell proliferation in Arabidopsis bioRxiv (2016) DOI: 10.1101/090563
The characteristic shapes and sizes of organs are established by cell proliferation patterns and final cell sizes, but the underlying molecular mechanisms coordinating these are poorly understood. Here we characterize a ubiquitin-activated peptidase called DA1 that limits the duration of cell proliferation during organ growth in Arabidopsis thaliana. The peptidase is activated by two RING E3 ligases, BB and DA2, which are subsequently cleaved by the activated peptidase and destabilized. In the case of BB, cleavage leads to destabilization by the RING E3 ligase PRT1 of the N-end rule pathway. DA1 peptidase activity also cleaves the de-ubiquitylase UBP15, which promotes cell proliferation, and the transcription factors TCP15 and TCP22, which promote cell proliferation proliferation and repress endoreduplication. We propose that DA1 peptidase activity regulates the duration of cell proliferation and the transition to endoreduplication and differentiation during organ formation in plants by coordinating the destabilization of regulatory proteins.
