TY - JOUR
T1 - Cullin-containing E3 ubiquitin ligases in plant development
AU - Schwechheimer, Claus
AU - Villalobos, Luz Irina A.Calderón
N1 - Funding Information:
We would like to thank D Weijers for his insightful comments on this review. Research in our laboratory is supported by the Deutsche Forschungsgemeinschaft and the Centre for Plant Molecular Biology at Tübingen University.
PY - 2004/12
Y1 - 2004/12
N2 - In eukaryotes, the ubiquitin-proteasome system participates in the control of signal transduction events by selectively eliminating regulatory proteins. E3 ubiquitin ligases specifically bind degradation substrates and mediate their poly-ubiquitylation, a prerequisite for their degradation by the 26S proteasome. On the basis of the analysis of the Arabidopsis genome sequence, it is predicted that there are more than 1000 E3 ubiquitin ligases in plants. Several types of E3 ubiquitin ligases have already been characterized in eukaryotes. Recently, some of these E3 enzymes have been implicated in specific plant signaling pathways.
AB - In eukaryotes, the ubiquitin-proteasome system participates in the control of signal transduction events by selectively eliminating regulatory proteins. E3 ubiquitin ligases specifically bind degradation substrates and mediate their poly-ubiquitylation, a prerequisite for their degradation by the 26S proteasome. On the basis of the analysis of the Arabidopsis genome sequence, it is predicted that there are more than 1000 E3 ubiquitin ligases in plants. Several types of E3 ubiquitin ligases have already been characterized in eukaryotes. Recently, some of these E3 enzymes have been implicated in specific plant signaling pathways.
UR - http://www.scopus.com/inward/record.url?scp=6044254445&partnerID=8YFLogxK
U2 - 10.1016/j.pbi.2004.09.009
DO - 10.1016/j.pbi.2004.09.009
M3 - Review article
C2 - 15491916
AN - SCOPUS:6044254445
SN - 1369-5266
VL - 7
SP - 677
EP - 686
JO - Current Opinion in Plant Biology
JF - Current Opinion in Plant Biology
IS - 6
ER -