CUL5

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Cullin 5
Protein CUL5 PDB 3DPL.png
Rendering based on PDB 3DPL.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CUL5 ; VACM-1; VACM1
External IDs OMIM601741 MGI1922967 HomoloGene2597 GeneCards: CUL5 Gene
RNA expression pattern
PBB GE CUL5 203531 at tn.png
PBB GE CUL5 203532 x at tn.png
PBB GE CUL5 203533 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8065 75717
Ensembl ENSG00000166266 ENSMUSG00000032030
UniProt Q93034 Q9D5V5
RefSeq (mRNA) NM_003478 NM_001161618
RefSeq (protein) NP_003469 NP_001155090
Location (UCSC) Chr 11:
107.88 – 107.98 Mb
Chr 9:
53.61 – 53.67 Mb
PubMed search [1] [2]

Cullin-5 is a protein that in humans is encoded by the CUL5 gene.[1][1][2][2][3]

Discovery[edit]

The mammalian gene product was originally discovered by expression cloning, due to the protein's ability to mobilize intracellular calcium in response to the peptide hormone arginine vasopressin. It was first titled VACM-1, for vasopressin-activated, calcium-mobilizing receptor.[4] Since then, VACM-1 has been shown to be homologous to the Cullin family of proteins, and was subsequently dubbed cul5.

Tissue distribution[edit]

Studies have shown that the cul5 protein is expressed at its highest levels in heart and skeletal tissue, and is specifically expressed in vascular endothelium and renal collecting tubules.[5]

Function[edit]

Cul5 inhibits cellular proliferation, potentially through its involvement in the SOCS/ BC-box/ eloBC/ cul5/ RING E3 ligase complex, which functions as part of the ubiquitin system for protein degradation.[6]

One study have shown that Cul5 plays a role in Reelin signaling cascade, participating in the DAB1 degradation and thus ensuring the negative feedback mechanism of Reelin signaling during corticogenesis.[7]

Interactions[edit]

CUL5 has been shown to interact with RBX1.[8][9]

References[edit]

  1. ^ a b Kipreos ET, Lander LE, Wing JP, He WW, Hedgecock EM (Aug 1996). "cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family". Cell 85 (6): 829–39. doi:10.1016/S0092-8674(00)81267-2. PMID 8681378. 
  2. ^ a b Byrd PJ, Stankovic T, McConville CM, Smith AD, Cooper PR, Taylor AM (May 1997). "Identification and analysis of expression of human VACM-1, a cullin gene family member located on chromosome 11q22-23". Genome Res 7 (1): 71–5. doi:10.1101/gr.7.1.71. PMID 9037604. 
  3. ^ "Entrez Gene: CUL5 cullin 5". 
  4. ^ Burnatowska-Hledin MA, Spielman WS, Smith WL, et al. (1995). "Expression cloning of an AVP-activated, calcium-mobilizing receptor from rabbit kidney medulla". Am J Physiol 268 (6): F1198–210. PMID 7611460. 
  5. ^ Burnatowska-Hledin M, Lazdins IB, Listenberger L, et al. (1999). "VACM-1 receptor is specifically expressed in rabbit vascular endothelium and renal collecting tubule". Am J Physiol 276 (2 Pt 2): F199–209. PMID 9950950. 
  6. ^ Petroski MD, Deshaies RJ. (2005). "Function and regulation of cullin-RING E3 ligases". Nature Reviews Molecular Cell Biology 6 (1): 9–21. doi:10.1038/nrm1547. PMID 15688063. 
  7. ^ Feng L, Allen NS, Simo S, Cooper JA (November 2007). "Cullin 5 regulates Dab1 protein levels and neuron positioning during cortical development". Genes Dev. 21 (21): 2717–30. doi:10.1101/gad.1604207. PMC 2045127. PMID 17974915. 
  8. ^ Duda, David M; Borg Laura A; Scott Daniel C; Hunt Harold W; Hammel Michal; Schulman Brenda A (Sep 2008). "Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation". Cell (United States) 134 (6): 995–1006. doi:10.1016/j.cell.2008.07.022. PMC 2628631. PMID 18805092. 
  9. ^ Ohta, T; Michel J J; Schottelius A J; Xiong Y (Apr 1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity". Mol. Cell (UNITED STATES) 3 (4): 535–41. doi:10.1016/S1097-2765(00)80482-7. ISSN 1097-2765. PMID 10230407. 

Further reading[edit]