Words similar to ligases
Example sentences for: ligases
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Many RING-finger-containing proteins that may act as ubiquitin ligases under certain conditions have otherwise diverse structures and functions [ 32 ] . It is clear that Siah can act in the ubiquitin pathway, targeting some proteins for proteolysis, under certain circumstances.
A number of RING finger proteins have recently been shown to act as E3 ubiquitin ligases [ 24 ] . WD40 domains have also been frequently found in E3 complexes as substrate recruiting domains [ 25 26 27 28 ] . Despite compelling evidence from Arabidopsis implying that COP1 may mediate protein degradation [ 4 5 ] , no direct evidence of COP1 participating in ubiquitination has been reported.
Within the past few years, the RING finger motif has emerged as a core structure feature for many ubiquitin ligases (E3s) [ 52 ] . In most cases, RING fingers function as E2 recruiting domains, and by directly interacting with E2s, bring E2s in the vicinity of ubiquitination substrates, which bind to other parts of the RING finger proteins or other subunits of the RING finger protein containing complexes.
In particular, one subunit—Csn5—moderates SCF (Skp1–cullin–F box) and other cullin-based E3 ubiquitin ligases by removal of the ubiquitin-like Rub1/Nedd8 molecule from the cullin subunit of the ligase complex.
In addition to the key roles in E3 ligase activity, RING finger domains have also been shown to be important for regulating subcellular localization of E3s and/or their substrates in a number of cases [ 53 54 55 56 ] . Studies have shown the MDM2 RING finger domain is required to promote nuclear export of p53 and this activity of MDM2 RING finger seems to be coupled with its ability to promote ubiquitination of p53 [ 53 54 55 ] . Rbx1/ROC1, the small RING finger subunit of the SCF E3 complexes, promotes the nuclear accumulation of Cul1, another subunit of the SCF complexes [ 56 ] . These studies have suggested a correlation between the ubiquitination activities of RING fingers and their roles in regulating subcellular localization of the E3 ligases which they are part of.