A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
By Simona Polo, S. Sigismund, M. Faretta, M. Guidi, M. Capua, G. Bossi, Hong Chen, P. Camilli, Pier Paolo Di Fiore. Nature, 2002
687 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/7529bab8702feedf389de6f06baed467ba2ec4eb
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Citations in the corpus
- Ubiquitylation and cell signaling (2005, background): “Several UBD-containing proteins are monoubiquitylated themselves, and importantly, their UBDs are required for their own monoubiquitylation (Polo et al, 2002; Shih et al, 2003).”
- Receptor downregulation and multivesicular-body sorting (2002, background): “pl?O14964">Hrs (hepatocyte growth factor-regulated tyrosine kinase substrate), which is also mono-ubiquitylate”
- Building ubiquitin chains: E2 enzymes at work (2009, background): “An intriguing example of this type of interaction is the coupled monoubiquitylation that is observed for many regulators of endocytosi”
- Reading protein modifications with interaction domains (2006, background): “UBD-containing proteins are themselves often monoubiquitylated in a manner that requires their UB”
- Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes (2006, neutral): “"”
- The ubiquitin code. (2012, background): “Lys63-linked chains activate IKK by promoting its binding to the upstream TAK1 that distinct types of ubiquitin topologies, i.e., Met1-, Lys11/Lys63-, Lys63-, or Lys48-linked chains, regulate signaling through inhibitor degradation, proteasomal processing, allosteric”
- The ESCRT pathway. (2011, background): “The ESCRT-0 subunit Vps27/Hrs is monoubiquitinated (Polo et al., 2002), although this ubiquitination is notessential forVps27 function, and toour knowledge, itsphysiological significance is unknown (Stringer and Piper, 2011).”