RING Finger Domain

2011 ◽  
pp. 3309-3309
Keyword(s):  
Ring Finger ◽  
Ring Finger Domain

scholarly journals Normal Immune System Development in Mice Lacking the Deltex-1 RING Finger Domain

2005 ◽  
Vol 25 (4) ◽  
pp. 1437-1445 ◽  
Author(s):  
Sébastien Storck ◽  
Frédéric Delbos ◽  
Nicolas Stadler ◽  
Catherine Thirion-Delalande ◽  
Florence Bernex ◽  
...  
Keyword(s):  
B Cell ◽  
Notch Signaling ◽  
Ubiquitin Ligase ◽  
Cell Lineage ◽  
Ring Finger ◽  
Mouse Development ◽  
Ring Finger Domain ◽  
Ubiquitin Ligase Activity ◽  
Immune System Development ◽  
Cell Commitment

ABSTRACT The Notch signaling pathway controls several cell fate decisions during lymphocyte development, from T-cell lineage commitment to the peripheral differentiation of B and T lymphocytes. Deltex-1 is a RING finger ubiquitin ligase which is conserved from Drosophila to humans and has been proposed to be a regulator of Notch signaling. Its pattern of lymphoid expression as well as gain-of-function experiments suggest that Deltex-1 regulates both B-cell lineage and splenic marginal-zone B-cell commitment. Deltex-1 was also found to be highly expressed in germinal-center B cells. To investigate the physiological function of Deltex-1, we generated a mouse strain lacking the Deltex-1 RING finger domain, which is essential for its ubiquitin ligase activity. Deltex-1Δ/Δ mice were viable and fertile. A detailed histological analysis did not reveal any defects in major organs. T- and B-cell development was normal, as were humoral responses against T-dependent and T-independent antigens. These data indicate that the Deltex-1 ubiquitin ligase activity is dispensable for mouse development and immune function. Possible compensatory mechanisms, in particular those from a fourth Deltex gene identified during the course of this study, are also discussed.

The MDM2 RING-finger domain is required to promote p53 nuclear export

2000 ◽  
Vol 2 (9) ◽  
pp. 569-573 ◽  
Author(s):  
Rory K. Geyer ◽  
Zhong K. Yu ◽  
Carl G. Maki
Keyword(s):  
Nuclear Export ◽  
Ring Finger ◽  
Ring Finger Domain

scholarly journals MdmX Protects p53 from Mdm2-Mediated Degradation

2000 ◽  
Vol 20 (3) ◽  
pp. 1001-1007 ◽  
Author(s):  
Mark W. Jackson ◽  
Steven J. Berberich
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Nuclear Export ◽  
P53 Protein ◽  
Ring Finger ◽  
Ring Finger Domain ◽  
Cycle Arrest ◽  
Dependent Cell ◽  
Potential Basis ◽  
P53 Tumor Suppressor Protein

ABSTRACT The p53 tumor suppressor protein is stabilized in response to cellular stress, resulting in activation of genes responsible for either cell cycle arrest or apoptosis. The cellular pathway for releasing normal cells from p53-dependent cell cycle arrest involves the Mdm2 protein. Recently, a p53-binding protein with homology to Mdm2 was identified and called MdmX. Like Mdm2, MdmX is able to bind p53 and inhibit p53 transactivation; however, the ability of MdmX to degrade p53 has yet to be examined. We report here that MdmX is capable of associating with p53 yet is unable to facilitate nuclear export or induce p53 degradation. In addition, expression of MdmX can reverse Mdm2-targeted degradation of p53 while maintaining suppression of p53 transactivation. Using a series of MdmX deletions, we have determined that there are two distinct domains of the MdmX protein that can stabilize p53 in the presence of Mdm2. One domain requires MdmX interaction with p53 and results in the retention of both proteins within the nucleus and repression of p53 transactivation. The second domain involves the MdmX ring finger and results in stabilization of p53 and an increase in p53 transactivation. The potential basis for stabilization and increased p53 transactivation by the MdmX ring finger domain is discussed. Based on these observations, we propose that the MdmX protein may function to maintain a nuclear pool of p53 protein in undamaged cells.

scholarly journals The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML.

1995 ◽  
Vol 14 (7) ◽  
pp. 1532-1541 ◽  
Author(s):  
K.L. Borden ◽  
M.N. Boddy ◽  
J. Lally ◽  
N.J. O'Reilly ◽  
S. Martin ◽  
...  
Keyword(s):  
Acute Promyelocytic Leukaemia ◽  
Solution Structure ◽  
Ring Finger ◽  
Promyelocytic Leukaemia ◽  
Ring Finger Domain

scholarly journals The AAA+ ATPase/ubiquitin ligase mysterin stabilizes cytoplasmic lipid droplets

2019 ◽  
Vol 218 (3) ◽  
pp. 949-960 ◽  
Author(s):  
Munechika Sugihara ◽  
Daisuke Morito ◽  
Shiori Ainuki ◽  
Yoshinobu Hirano ◽  
Kazutoyo Ogino ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Lipid Droplets ◽  
Ring Finger ◽  
Unknown Etiology ◽  
Cerebrovascular Disorder ◽  
Intracellular Protein ◽  
Ring Finger Domain ◽  
Genetic Studies ◽  
Aaa Atpase ◽  
Potential Link

Mysterin, also known as RNF213, is an intracellular protein that forms large toroidal oligomers. Mysterin was originally identified in genetic studies of moyamoya disease (MMD), a rare cerebrovascular disorder of unknown etiology. While mysterin is known to exert ubiquitin ligase and putative mechanical ATPase activities with a RING finger domain and two adjacent AAA+ modules, its biological role is poorly understood. Here, we report that mysterin is targeted to lipid droplets (LDs), ubiquitous organelles specialized for neutral lipid storage, and markedly increases their abundance in cells. This effect was exerted primarily through specific elimination of adipose triglyceride lipase (ATGL) from LDs. The ubiquitin ligase and ATPase activities of mysterin were both important for its proper LD targeting. Notably, MMD-related mutations in the ubiquitin ligase domain of mysterin significantly impaired its fat-stabilizing activity. Our findings identify a unique new regulator of cytoplasmic LDs and suggest a potential link between the pathogenesis of MMD and fat metabolism.

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