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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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BH3-ligand regulates access of MCL-1 to its E3 ligase.

A genome wide search for new BH3-containing Bcl-2 family members was conducted using position weight matrices (PWM) and identified a large (480kDa), novel BH3-only protein, originally called LASU1 (now also known as Ureb-1, E3(histone), ARF-BP1, and Mule). We demonstrated that LASU1 is an E3 ligase that ubiquitinated Mcl-1 in vitro and was required for its proteasome-dependent degradation in HeLa cells. Of note, the BH3 domain of LASU1 interacted with Mcl-1 but not with Bcl-2 or Bcl-Xl. A competing BH3-ligand derived from Bim interacted with Mcl-1 and prevented its interaction with LASU1 in HeLa cells, causing elevation of the steady-state levels of Mcl-1. This suggests that the unliganded form of Mcl-1 is sensitive to LASU1-mediated degradation of Mcl-1.[1]

References

  1. BH3-ligand regulates access of MCL-1 to its E3 ligase. Warr, M.R., Acoca, S., Liu, Z., Germain, M., Watson, M., Blanchette, M., Wing, S.S., Shore, G.C. FEBS Lett. (2005) [Pubmed]
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