Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
作者： Daniel Finley
DOI: 10.1146/ANNUREV.BIOCHEM.78.081507.101607
关键词: Protein degradation 、 Deubiquitination 、 Ubiquitin 、 Cell biology 、 Proteasome 、 Proteasome assembly 、 Ubiquitin-conjugating enzyme 、 Biochemistry 、 Biology 、 Ubiquitin ligase 、 Deubiquitinating enzyme
摘要: The proteasome is an intricate molecular machine, which serves to degrade proteins following their conjugation to ubiquitin. Substrates dock onto the proteasome at its 19-subunit regulatory particle via a diverse set of ubiquitin receptors and are then translocated into an internal chamber within the 28-subunit proteolytic core particle (CP), where they are hydrolyzed. Substrate is threaded into the CP through a narrow gated channel, and thus translocation requires unfolding of the substrate. Six distinct ATPases in the regulatory …
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