RING Fingers as

It was also found that Rbxl was central to the E3 activity of the newly described complex [40, 41]. During this time, others demonstrated binding 

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Goncyy Their molecular nature is completely different. PAR-3 is a PDZ-containing protein that has Bazooka and ASIP as Drosophila and mammalian cousins, respectively (Izumi et al 1998, Kuchinke et al 1998). PAR-2 is a ring-finger containing protein that does not have a characterized Drosophila or mammalian orthologue. 

Thomas Cbl is a ring finger protein which is involved in down-regulation of the receptor. This didn t fall out of the original screen. Are there mutants in Cbl as well ... 

Remarkably, at the same time, several groups independently determined that there was a previously undiscovered component to the SCF complex - a small non-canonical RING finger protein known variably as Rbxl, Rod or Hrtl [36-... 

RING finger proteins may have other domains associated with signal transduction, such as SH3 and STAT domains and domains that bind and effect hydrolysis of nucleotides in signal transduction or for other purposes. These include ATPases, ATP synthases, serine/threonine kinases, GTP-binding domains, ADP-ribosylation domains and AAA-superfamily ATPases (http //home.cancer.gov/lpds/weissman). 

The coiled-coil domain frequently mediates hetero- or homodimerization. About two-thirds of a large number of TRIM proteins tested dimerize [125]. As a number of other RING finger proteins either homo- or hererodimerize, dimerization may facilitate optimal E3 activity of TRIMs. While most proteins that carry the TRIM... 

The sine qua non of the lAPs (inhibitors of apoptosis) is one or more copies of a Zn-finger-containrng domain referred to as a BIR (Baculovirus ZAP Repeat Figure 4.4C). This name was derived from their initial identification in baculovirus, where they prevent host-cell apoptosis, allowing viral replication. At least 10 mammalian lAPs have been described. Many have C-terminal RING fingers [153]. A major... 

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