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Gene Review

CUL5  -  cullin 5

Homo sapiens

Synonyms: CUL-5, Cullin-5, VACM-1, VACM1, Vasopressin-activated calcium-mobilizing receptor 1
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Disease relevance of CUL5


High impact information on CUL5

  • Therefore, selective assembly with Cul5 versus Cul2 E3 may require protein interfaces besides the SOCS-box-ElonginC interaction [4].
  • This new motif was necessary but insufficient for interaction with Cul5-ElonginB-ElonginC, as two highly conserved Cys residues outside the SOCS box were required to interact with Cul5 but not ElonginC [4].
  • However, although the nature and expression of both vasopressin V1 receptors and human VACM are apparently unaffected by dedifferentiation in SCCL, only the abnormal (and probably nonfunctional) form of the V2 receptor could be demonstrated in variant cell line NCI H82 [5].
  • Identification and analysis of expression of human VACM-1, a cullin gene family member located on chromosome 11q22-23 [2].
  • We have determined the complete amino acid sequence of the human Hs-VACM-1 protein, which is 780 amino acids long [2].

Chemical compound and disease context of CUL5


Biological context of CUL5


Anatomical context of CUL5


Associations of CUL5 with chemical compounds

  • Mutations of His/Cys residues in the HCCH motif impair zinc coordination, Cul5 binding, and APOBEC3G degradation [7].
  • The protein kinase C specific inhibitor Gö-6983 further enhanced the inhibitory effect of VACM-1 on AVP-stimulated cAMP production [13].
  • A randomized trial comparing Vincristine, Adriamycin, Cyclophosphamide (VAC) with or without Methotrexate with citrovorum factor rescue (VACM) was performed in 64 patients with metastatic postmenopausal mammary carcinoma [14].

Physical interactions of CUL5


Regulatory relationships of CUL5

  • Mutations of conserved hydrophobic residues (Ile-120, Ala-123, and Leu-124) located between the two Cys residues in the HCCH motif disrupt binding of the zinc-coordinating region to Cul5 and inhibit APOBEC3G degradation [7].
  • Screening with the Human PathwayFinder-1 GEArray system and subsequent Western blot analysis demonstrated that VACM-1 induces p53 mRNA and protein expression [10].

Other interactions of CUL5

  • These findings suggest that the E3 ubiquitin ligase activity of the Vif-BC-Cul5 complex is essential for Vif function against APOBEC3G [15].
  • At present, the determinants of Cul2 vs. Cul5 specificity for the BC-box-containing receptors are poorly defined [16].
  • Zinc chelation had no effect on cellular Cul5-SOCS3 E3 ligase assembly, suggesting that zinc-dependent E3 ligase assembly may be unique to HIV-1 Vif, representing a new target for novel drug design [17].
  • The contact with knitted Dacron did not induce significant variations of ICAM-1 and VACM-1 [18].
  • At 4 h ICAM-1 and E-selectin, but not VACM-1, were stimulated by both IL-1beta and TNF-alpha [19].

Analytical, diagnostic and therapeutic context of CUL5

  • Immunocytochemistry studies demonstrated that VACM-1 was expressed in 0.6-6% of the T47D cells and localized to the nucleus of mitotic cells [3].
  • RT-PCR experiments show the expression of V1a, V1b, V2 and vasopressin-activated calcium-mobilizing (VACM) receptors mRNAs [20].
  • To characterize the VACM-1 receptor, we examined its tissue-specific expression using Northern blot, RT-PCR, and immunostaining analyses [21].
  • DESIGN AND METHODS: To clarify this issue, we evaluated the effect of C-peptide on VACM-1 RNA (measured by semiquantitative RT-PCR) and protein expression (measured by immunoblotting) in human skin fibroblasts (where a specific binding of C-peptide was demonstrated) and in human mesangial cells, the cellular target of diabetic nephropathy [6].
  • Combination chemotherapy in advanced postmenopausal mammary carcinoma. A comparison between VAC and VACM therapy [14].


  1. Polymorphisms of CUL5 are associated with CD4+ T cell loss in HIV-1 infected individuals. An, P., Duggal, P., Wang, L.H., O'Brien, S.J., Donfield, S., Goedert, J.J., Phair, J., Buchbinder, S., Kirk, G.D., Winkler, C.A. PLoS Genet. (2007) [Pubmed]
  2. Identification and analysis of expression of human VACM-1, a cullin gene family member located on chromosome 11q22-23. Byrd, P.J., Stankovic, T., McConville, C.M., Smith, A.D., Cooper, P.R., Taylor, A.M. Genome Res. (1997) [Pubmed]
  3. T47D breast cancer cell growth is inhibited by expression of VACM-1, a cul-5 gene. Burnatowska-Hledin, M.A., Kossoris, J.B., Van Dort, C.J., Shearer, R.L., Zhao, P., Murrey, D.A., Abbott, J.L., Kan, C.E., Barney, C.C. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  4. Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Yu, Y., Xiao, Z., Ehrlich, E.S., Yu, X., Yu, X.F. Genes Dev. (2004) [Pubmed]
  5. Expression of all known vasopressin receptor subtypes by small cell tumors implies a multifaceted role for this neuropeptide. North, W.G., Fay, M.J., Longo, K.A., Du, J. Cancer Res. (1998) [Pubmed]
  6. C-peptide increases the expression of vasopressin-activated calcium-mobilizing receptor gene through a G protein-dependent pathway. Maestroni, A., Ruggieri, D., Dell'Antonio, G., Luzi, L., Zerbini, G. Eur. J. Endocrinol. (2005) [Pubmed]
  7. A zinc-binding region in Vif binds Cul5 and determines cullin selection. Mehle, A., Thomas, E.R., Rajendran, K.S., Gabuzda, D. J. Biol. Chem. (2006) [Pubmed]
  8. Construction of a transcription map around the gene for ataxia telangiectasia: identification of at least four novel genes. Stankovic, T., Byrd, P.J., Cooper, P.R., McConville, C.M., Munroe, D.J., Riley, J.H., Watts, G.D., Ambrose, H., McGuire, G., Smith, A.D., Sutcliffe, A., Mills, T., Taylor, A.M. Genomics (1997) [Pubmed]
  9. Adenovirus ubiquitin-protein ligase stimulates viral late mRNA nuclear export. Woo, J.L., Berk, A.J. J. Virol. (2007) [Pubmed]
  10. VACM-1, a cul-5 gene, inhibits cellular growth by a mechanism that involves MAPK and p53 signaling pathways. Van Dort, C., Zhao, P., Parmelee, K., Capps, B., Poel, A., Listenberger, L., Kossoris, J., Wasilevich, B., Murrey, D., Clare, P., Burnatowska-Hledin, M. Am. J. Physiol., Cell Physiol. (2003) [Pubmed]
  11. Expression of VACM-1 protein in cultured rat adrenal endothelial cells is linked to the cell cycle. Burnatowska-Hledin, n.u.l.l., Zeneberg, A., Roulo, A., Grobe, J., Zhao, P., Lelkes, P.I., Clare, P., Barney, C. Endothelium (2001) [Pubmed]
  12. Analysis of CUL-5 expression in breast epithelial cells, breast cancer cell lines, normal tissues and tumor tissues. Fay, M.J., Longo, K.A., Karathanasis, G.A., Shope, D.M., Mandernach, C.J., Leong, J.R., Hicks, A., Pherson, K., Husain, A. Mol. Cancer (2003) [Pubmed]
  13. VACM-1, a cullin gene family member, regulates cellular signaling. Burnatowska-Hledin, M., Zhao, P., Capps, B., Poel, A., Parmelee, K., Mungall, C., Sharangpani, A., Listenberger, L. Am. J. Physiol., Cell Physiol. (2000) [Pubmed]
  14. Combination chemotherapy in advanced postmenopausal mammary carcinoma. A comparison between VAC and VACM therapy. Mattsson, W., Arwidi, A., von Eyben, F., Lindholm, C.E. Acta radiologica: oncology, radiation, physics, biology. (1979) [Pubmed]
  15. Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. Kobayashi, M., Takaori-Kondo, A., Miyauchi, Y., Iwai, K., Uchiyama, T. J. Biol. Chem. (2005) [Pubmed]
  16. Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Luo, K., Xiao, Z., Ehrlich, E., Yu, Y., Liu, B., Zheng, S., Yu, X.F. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  17. Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G. Xiao, Z., Ehrlich, E., Luo, K., Xiong, Y., Yu, X.F. FASEB J. (2007) [Pubmed]
  18. Expression of adhesion molecules on endothelial cells after contact with knitted Dacron. Cenni, E., Granchi, D., Ciapetti, G., Verri, E., Cavedagna, D., Gamberini, S., Cervellati, M., Di Leo, A., Pizzoferrato, A. Biomaterials (1997) [Pubmed]
  19. Poly ADP ribose-polymerase inhibitors prevent the upregulation of ICAM-1 and E-selectin in response to Th1 cytokine stimulation. Sharp, C., Warren, A., Oshima, T., Williams, L., Li, J.H., Alexander, J.S. Inflammation (2001) [Pubmed]
  20. Vasotocin and vasopressin stimulation of the chloride secretion in the human bronchial epithelial cell line, 16HBE14o-. Bernard, K., Bogliolo, S., Ehrenfeld, J. Br. J. Pharmacol. (2005) [Pubmed]
  21. VACM-1 receptor is specifically expressed in rabbit vascular endothelium and renal collecting tubule. Burnatowska-Hledin, M., Lazdins, I.B., Listenberger, L., Zhao, P., Sharangpani, A., Folta, V., Card, B. Am. J. Physiol. (1999) [Pubmed]
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