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2012 ; 7
(1
): 52-63
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Unraveling the complexity of ubiquitin signaling
#MMPMID22196026
Strieter ER
; Korasick DA
ACS Chem Biol
2012[Jan]; 7
(1
): 52-63
PMID22196026
show ga
Protein ubiquitination, the covalent attachment of ubiquitin to target proteins,
has emerged as one of the most prevalent posttranslational modifications (PTMs),
regulating nearly every cellular pathway. The diversity of signaling associated
with this particular PTM stems from the myriad ways in which a target protein can
be modified by ubiquitin, e.g., monoubiquitin, multi-monoubiquitin, and
polyubiquitin linkages. In this Review, we focus on developments in both
enzymatic and chemical methods that engender ubiquitin with new chemical and
physical properties. Moreover, we highlight how these methods have enabled
studies directed toward (i) characterizing enzymes responsible for reversing the
ubiquitin modification, (ii) understanding the influence of ubiquitin on protein
function and crosstalk with other PTMs, and (iii) uncovering the impact of
polyubiquitin chain linkage and length on downstream signaling events.
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