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Gene Review

Ubb  -  ubiquitin B

Rattus norvegicus

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Disease relevance of Ubb

  • Muscle atrophy appears to be caused by changes in mRNA levels of specific regulators of proteolysis, protein synthesis, and contractile apparatus assembling, such as polyubiquitin, elongation factor 2, and nebulin [1].

High impact information on Ubb

  • The combined results suggest that the normally rapid proteasome degradation of translocation-arrested apoB can be regulated by a sterol-sensitive polyubiquitin conjugation step in the endoplasmic reticulum [2].
  • This, and the finding that the developmental induction of expression of polyubiquitin (UbC) mirrors that of VSMC contractile proteins, suggests that ubiquitin, a protein known to associate with and degrade contractile proteins in skeletal muscle, is involved in the function or maintenance of the contractile phenotype of VSMCs [3].
  • In situ hybridisation of the polyubiquitin riboprobe to sections of diseased human coronary arteries indicated much higher expression in medial than in intimal VSMCs [3].
  • Polyubiquitin is a new phenotypic marker of contractile vascular smooth muscle cells [3].
  • During starvation, polyUb mRNA levels also increased in heart, but not in liver, kidney, spleen, fat, brain or testes [4].

Biological context of Ubb


Anatomical context of Ubb

  • Only polyubiquitin (UbC) mRNA increased markedly following ischaemia in the central zone of the MCA territory of the neocortex [8].
  • This indicates relatively large amounts of polyubiquitin complex associated with sarcomeric actin in muscle fibers in early stages of intoxication [9].
  • Based on these results it seems that actin is an important target in organophosphate-induced myofiber degradation and that the degradation of this protein-by the polyubiquitin pathway-may play an important role in the early disorganization of the sarcomere, as observed by electron microscopy [9].

Associations of Ubb with chemical compounds

  • Two proteasome inhibitors, a peptidyl aldehyde and an epoxy ketone, which cause accumulation of ubiquitinated proteins, were found to enhance expression of stress-inducible genes, including HSP70i and the polyubiquitin genes UbB and UbC [10].

Other interactions of Ubb

  • The mRNA contents of polyubiquitin and the ubiquitin ligases muscle atrophy F-box (MAFbx)/Atrogin-1 and muscle RING finger 1 (MuRF1) were elevated in immobilized muscle at all time points, with peak expression occurring at day 3 [11].
  • METHODS AND RESULTS: In a model of atrophic remodeling induced by heterotopic transplantation of the rat heart, we measured gene transcription, protein expression, polyubiquitin content, and regulators of the mTOR pathway at 2, 4, 7, and 28 days [12].
  • Especially stathmin, polyubiquitin and heterogeneous nuclear ribonucleoprotein seem to play an important role in pre- and postnatal development [13].

Analytical, diagnostic and therapeutic context of Ubb

  • Northern blot analysis showed that this polyubiquitin was more highly expressed in differentiated, freshly dispersed rat and human aortic VSMCs compared with their dedifferentiated proliferating counterparts [3].
  • After denervation of the soleus, there was a progressive 2-3-fold increase in polyUb mRNA for 1-3 days, whereas total RNA content fell [4].
  • Bands of polyubiquitin complexes in muscle homogenates were observed by immunoblotting [9].


  1. Characterization of control and immobilized skeletal muscle: an overview from genetic engineering. St-Amand, J., Okamura, K., Matsumoto, K., Shimizu, S., Sogawa, Y. FASEB J. (2001) [Pubmed]
  2. Translocation-arrested apolipoprotein B evades proteasome degradation via a sterol-sensitive block in ubiquitin conjugation. Du, E.Z., Fleming, J.F., Wang, S.L., Spitsen, G.M., Davis, R.A. J. Biol. Chem. (1999) [Pubmed]
  3. Polyubiquitin is a new phenotypic marker of contractile vascular smooth muscle cells. Adam, P.J., Weissberg, P.L., Cary, N.R., Shanahan, C.M. Cardiovasc. Res. (1997) [Pubmed]
  4. Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy. Medina, R., Wing, S.S., Goldberg, A.L. Biochem. J. (1995) [Pubmed]
  5. Nucleotide sequence and expression of the rat polyubiquitin mRNA. Hayashi, T., Noga, M., Matsuda, M. Biochim. Biophys. Acta (1994) [Pubmed]
  6. Characterization and expression of two chicken cDNAs encoding ubiquitin fused to ribosomal proteins of 52 and 80 amino acids. Mezquita, J., Pau, M., Mezquita, C. Gene (1997) [Pubmed]
  7. Conjugation of phenylalanine hydroxylase with polyubiquitin chains catalysed by rat liver enzymes. Døskeland, A.P., Flatmark, T. Biochim. Biophys. Acta (2001) [Pubmed]
  8. Gene expressions of ubiquitin and hsp70 following focal ischaemia in rat brain. Noga, M., Hayashi, T., Tanaka, J. Neuroreport (1997) [Pubmed]
  9. Early expression of ubiquitin in myofibers of rats in organophosphate intoxication. Calore, E.E., Sesso, A., Puga, F.R., Cavaliere, M.J., Calore, N.M., Weg, R. Ecotoxicol. Environ. Saf. (1999) [Pubmed]
  10. Proteasome inhibition in neuronal cells induces a proinflammatory response manifested by upregulation of cyclooxygenase-2, its accumulation as ubiquitin conjugates, and production of the prostaglandin PGE(2). Rockwell, P., Yuan, H., Magnusson, R., Figueiredo-Pereira, M.E. Arch. Biochem. Biophys. (2000) [Pubmed]
  11. Hindlimb casting decreases muscle mass in part by proteasome-dependent proteolysis but independent of protein synthesis. Krawiec, B.J., Frost, R.A., Vary, T.C., Jefferson, L.S., Lang, C.H. Am. J. Physiol. Endocrinol. Metab. (2005) [Pubmed]
  12. Atrophic remodeling of the heart in vivo simultaneously activates pathways of protein synthesis and degradation. Razeghi, P., Sharma, S., Ying, J., Li, Y.P., Stepkowski, S., Reid, M.B., Taegtmeyer, H. Circulation (2003) [Pubmed]
  13. Proteome analysis of isolated myenteric plexus reveals significant changes in protein expression during postnatal development. Hagl, C.I., Thil, O., Holland-Cunz, S., Faissner, R., Wandschneider, S., Schnölzer, M., Löhr, M., Schäfer, K.H. Autonomic neuroscience : basic & clinical. (2005) [Pubmed]
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