Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation
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چکیده
منابع مشابه
Signal and Specificity of Protein Ubiquitination for Proteasomal Degradation
The eukaryotic ubiquitin system regulates essential cell events such as DNA repair, protein homeostasis, and signal transduction. Like many biochemical processes, ubiquitination must ensure signaling efficiency and in the meantime maintain substrate specificity. We examine this signal-specificity relationship by theoretical models of polyubiquitinations that tag proteins for the proteasomal deg...
متن کاملActivity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation.
Pupylation is a bacterial post-translational modification of target proteins on lysine residues with prokaryotic ubiquitin-like protein Pup. Pup-tagged substrates are recognized by a proteasome-interacting ATPase termed Mpa in Mycobacterium tuberculosis. Mpa unfolds pupylated substrates and threads them into the proteasome core particle for degradation. Interestingly, Mpa itself is also a pupyl...
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The mammalian 20S proteasome is a heterodimeric cylindrical complex (α7β7β7α7), composed of four rings each composed of seven different α or β subunits with broad proteolytic activity. We review the mammalian proteins shown to directly interact with specific 20S proteasomal subunits and those subjected to ubiquitin-independent proteasomal degradation (UIPD). The published reports of proteins th...
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Conjugation of ubiquitin to target proteins is a finely tuned process involving a reaction, culminating in the conjugation of a single ubiquitin (1). The first step is conjugation of a single ubiquitin molecule to the substrate’s protein amino group (monoubiquitination) or to multiple amino groups (multimonoubiquitination), which can remain as it is or be further extended by additional ubiquiti...
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ژورنال
عنوان ژورنال: PLOS ONE
سال: 2019
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0215439