Multisite phosphorylation dictates selective E2-E3 pairing as revealed by Ubc8/UBE2H-GID/CTLH assemblies
Chrustowicz, Sherpa, et al. decipher evolutionarily conserved determinants of an exquisitely specific E3-E2 partnership ubiquitylating globular substrates. Cryo-EM visualizes a flexing GID E3 superassembly channeling its substrate between two ubiquitylation active sites. The catalytic architecture depends on multivalent Ubc8/UBE2H-GID/CTLH E3 contacts, including between multiphosphorylated E2 extensions and complementary E3 basic patches.
Source: Molecular Cell - Category: Cytology Authors: Jakub Chrustowicz, Dawafuti Sherpa, Jerry Li, Christine R. Langlois, Eleftheria C. Papadopoulou, D. Tung Vu, Laura A. Hehl, Özge Karayel, Viola Beier, Susanne von Gronau, Judith Müller, J. Rajan Prabu, Matthias Mann, Gary Kleiger, Arno F. Alpi, Brenda A Tags: Article Source Type: research
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