Journal ArticleDOI
Mechanisms underlying ubiquitination.
TLDR
Recent findings reveal that all known E3s utilize one of just two catalytic domains--a HECT domain or a RING finger--and crystal structures have provided the first detailed views of an active site of each type.Abstract:
▪ Abstract The conjugation of ubiquitin to other cellular proteins regulates a broad range of eukaryotic cell functions. The high efficiency and exquisite selectivity of ubiquitination reactions reflect the properties of enzymes known as ubiquitin-protein ligases or E3s. An E3 recognizes its substrates based on the presence of a specific ubiquitination signal, and catalyzes the formation of an isopeptide bond between a substrate (or ubiquitin) lysine residue and the C terminus of ubiquitin. Although a great deal is known about the molecular basis of E3 specificity, much less is known about molecular mechanisms of catalysis by E3s. Recent findings reveal that all known E3s utilize one of just two catalytic domains—a HECT domain or a RING finger—and crystal structures have provided the first detailed views of an active site of each type. The new findings shed light on many aspects of E3 structure, function, and mechanism, but also emphasize that key features of E3 catalysis remain to be elucidated.read more
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Orthopoxviruses Require a Functional Ubiquitin-Proteasome System for Productive Replication
Alastair Teale,Stephanie Campbell,Nicholas van Buuren,Wendy C. Magee,Kelly Watmough,Brianne Couturier,Robyn Shipclark,Michele Barry +7 more
TL;DR: It is shown that poxvirus infection was dramatically affected by a range of proteasome inhibitors, including MG132, MG115, lactacystin, and bortezomib (Velcade), and the addition of an ubiquitin-activating enzyme (E1) inhibitor had a similar affect on late and early protein expression.
Journal ArticleDOI
Role of the ubiquitin conjugation system in the maintenance of mitochondrial homeostasis.
TL;DR: The role of ubiquitin (Ub) conjugation in the maintenance of mitochondrial function is discussed and it is found that at least four putative RING finger E3 Ub ligases, the main determinants of substrate specificity in the ubiquitination system, localize to mitochondria.
A thesis submitted in partial fulfillment of the requirements for the degree of
TL;DR: It is shown that P34 can function as an E3 ubiquitin ligase during OpMNPV infection and determines the role of host proteins in viral replication.
Journal ArticleDOI
Tobacco RING E3 Ligase NtRFP1 Mediates Ubiquitination and Proteasomal Degradation of a Geminivirus-Encoded βC1
TL;DR: Results suggest that tobacco RING E3 ligase NtRFP1 attenuates disease symptoms by interacting with βC1 to mediate its ubiquitination and degradation via the ubiquitin/26S proteasome system.
Journal ArticleDOI
The E3 ligase Itch is a negative regulator of the homeostasis and function of hematopoietic stem cells
TL;DR: It is shown that the E3 ubiquitin ligase Itch negatively regulated the development and function of HSCs, and was identified as a previously unknown negative regulator of H SC homeostasis and function.
References
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Journal ArticleDOI
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TL;DR: This review discusses recent information on functions and mechanisms of the ubiquitin system and focuses on what the authors know, and would like to know, about the mode of action of ubi...
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NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses
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The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Patrick H. Maxwell,Michael S. Wiesener,Gin-Wen Chang,Steven C. Clifford,Emma C. Vaux,Matthew Edward Cockman,Charles C. Wykoff,Christopher W. Pugh,Eamonn R. Maher,Peter J. Ratcliffe,Peter J. Ratcliffe +10 more
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Journal ArticleDOI
Mdm2 promotes the rapid degradation of p53
TL;DR: It is proposed that the Mdm2-promoted degradation of p53 provides a new mechanism to ensure effective termination of the p53 signal.