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Welcome to ZOMEBase, the information center for the three PCI Zomes: COP9 Signalosome, the regulatory lid of the 26S proteasome and eIF3

What is a ZOME?

A "ZOME" is any one of three related multi-protein complexes:

the Cop9 Signalosome
the Regulatory Lid of the 26S proteasome

These complexes were grouped together on the basis of similarities in their subunit composition and predicted structure. While subunits between the complexes share little primary sequence similarity, six subunits of all three complexes contain a PCI (Proteasome, CSN, eIF3) motif, while two subunits carry an MPN (Mpr1, Pad1, N-terminal) motif. This conserved six PCI / two MPN structure (among most higher eukaryotes) strongly suggests a common ancestor for these complexes. (1)

ZOMES, individually and in concert, affect proteome composition.

In ZOMEBase you can find

Want to contribute to ZOMEBase?

All Zomers are welcome and invited to contribute to and modify ZOMEBase using the Twiki editor on each page. To edit, you'll need a username and password. Please contact dannyc@tauex.tau.ac.il . As a contributer you can edit and add to exisiting content including making new pages.

Pages that need to be worked on

ZOMEBase Utilities

Recent ZOMES articles

NCBI: db=pubmed; Term=cop9 or "proteasome lid" or eIF3 or jab1
Related Articles

Inositol hexakisphosphate kinase-1 mediates assembly/disassembly of the CRL4-signalosome complex to regulate DNA repair and cell death.

Proc Natl Acad Sci U S A. 2014 Oct 27;

Authors: Rao F, Xu J, Khan AB, Gadalla MM, Cha JY, Xu R, Tyagi R, Dang Y, Chakraborty A, Snyder SH

Inositol polyphosphates containing an energetic pyrophosphate bond are formed primarily by a family of three inositol hexakisphosphate (IP6) kinases (IP6K1-3). The Cullin-RING ubiquitin ligases (CRLs) regulate diverse biological processes through substrate ubiquitylation. CRL4, comprising the scaffold Cullin 4A/B, the E2-interacting Roc1/2, and the adaptor protein damage-specific DNA-binding protein 1, is activated by DNA damage. Basal CRL4 activity is inhibited by binding to the COP9 signalosome (CSN). UV radiation and other stressors dissociate the complex, leading to E3 ligase activation, but signaling events that trigger signalosome dissociation from CRL4 have been unclear. In the present study, we show that, under basal conditions, IP6K1 forms a ternary complex with CSN and CRL4 in which IP6K1 and CRL4 are inactive. UV dissociates IP6K1 to generate IP7, which then dissociates CSN-CRL4 to activate CRL4. Thus, IP6K1 is a novel CRL4 subunit that transduces UV signals to mediate disassembly of the CRL4-CSN complex, thereby regulating nucleotide excision repair and cell death.

PMID: 25349427 [PubMed - as supplied by publisher]


1 : Hofmann, K., and Bucher, P. (1998). The pci domain: A common theme in three multi-protein complexes. Trends Biochem Sci 23, 204-205.;Aravind, L., and Ponting, C.P. (1998). Homologues of 26S proteasome subunits are regulators of transcription and translation. Protein Sci 7, 1250-1254.; Kim, T.-H., Hofmann, K., von Arnim, A.G., and Chamovitz, D.A. (2001). The pci complexes:pretty complex interations in diverse signaling pathways. Trend Plant Sciences 6, 379-386.

r21 - 02 Aug 2010 - 12:15:05 - IdoGan
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