Recognition of the polyubiquitin proteolytic signal

By Julia S. Thrower, L. Hoffman, M. Rechsteiner, C. Pickart. EMBO Journal, 2000

1,888 citations recorded by the source corpus.

Subfields: Cell Biology, Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/2f5d658589a44b7e0188185b4718baf46ccad8a6

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Citations in the corpus

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (2009, background): “Because longer ubiquitin chains seem to associate more tightly with the proteasome (101), chain extension should promote the degradation of attached substrates.”
Ubiquitin and proteasomes: Protein regulation by monoubiquitin (2001, background): “Multi-ubiquitin chains, in which the carboxy-terminal glycine of ubiquitin is linked to Lys48 of the preceding ubiquitin, mediate the best-characterized function of ubiquiti”
The Logic of the 26S Proteasome. (2017, positive): “For example, ubiquitylated DHFR is rapidly degraded in cells and in vitro; however, in the presence of its inhibitor, the widely-used drug methotrexate, DHFR assumes a tightly folded structure that prevents DHFR degradation (Johnston et al., 1995; Thrower et al., 2000).”
Origin and Function of Ubiquitin-like Protein Conjugation (2009, background): “The 26S proteasome is responsible for the degradation of polyubiquitylated proteins, and direct binding of a polyubiquitin chain to the proteasome can fully account for the observed affinity of model polyubiquitylated proteins for this protease comple”
Building ubiquitin chains: E2 enzymes at work (2009, background): “The substrate receptors of the 26S proteasome recognize ubiquitylated proteins only after a chain containing at least four ubiquitin molecules has been attache”
Degradation signal diversity in the ubiquitin-proteasome system (2008, neutral): “Several studies have indicated that in addition to tethering the substrate to the proteasome, the degron must also have a more loosely structured peptide segment that initiates unfolding and insertion into the proteasom”
Systematic exploration of ubiquitin sequence, E1 activation efficiency, and experimental fitness in yeast (2014, background): “Our display studies as well as follow up studies with individual ubiquitin mutations demonstrate that E1 can selectively filter ubiquitin protein molecules with substitutions at position 48 that cause known biochemical defects when activated and attached to substrates 58 .”
The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “Moreover, it has been reported that the K48-type Ub chain consisting of four Ubs can be degraded by the proteasome.(494,495) Why four Ubs? These lengths of the Ub chain are also required for other linkage Ub chains.”
Ubiquitin and ubiquitin-like proteins as multifunctional signals (2005, background): “4 ), to at least four sequentially attached ubiquitins, which is sufficient to allow the ubiquitylated target protein to be recognized and degraded by the 26S proteasom”
Regulation and Cellular Roles of Ubiquitin-specific Deubiquitinating Enzymes (2009, background): “from inhibition of the proteasome by excess unanchored polyubiquitin (125).”
The mitochondrial p53 pathway (2008, positive): “(Multi)-monoubiquitinated proteins are stable, since efficient proteasomal degradationminimally requires amultiubiquitin chain that is at least 4 subunits long per individual lysine residue [24].”