The N-terminal, TPR-containing domain of the mitotic checkpoint protein BUBR1 does not bind fatty acids

In the interesting and comprehensive article entitled Involvement of some large immunophilins and their ligands n the protection and regeneration of neurons: A hypothetical ode of action” signed by Galat (2006), the author quoted page 356): “Some TPR-rich domains are known to bind certain atty acids such as the BUBR1 protein (Bolanos-Garcia et al., 005)”. Although it is true that some TPR domains can bind atty acids, the statement is unfortunate, as we did not affirm hat BUBR1 exhibits such activity. The report cited by Dr. alat dealt with the description of an important local structure imilarity between the TPR motif of protein phosphatase 5 TPR-PP5) and that of BUBR1 despite the different functions f these proteins (Bolanos-Garcia et al., 2005). In one hand, he TPR motif of PP5 regulates the activity of the C-terminal hosphatase domain and mediates the interaction of this protein ith others such as cryptochromes CRY1 and CRY2 (Zhao and ancar, 1997) and the single transmembrane atrial natriuretic eptide receptor (Chinkers, 1994). On the other hand, BUBR1 also commonly referred to as BUB1B) is a multidomain protein hat plays an essential role in the mitotic checkpoint control by hosphorylation of critical cellular component(s) of the mitotic heckpoint pathway (Harris et al., 2005). In our report we ypothesized whether the putative TPR motif of the N-terminal omain of BUBR1 is involved in direct protein–protein and/or rotein–lipid interactions in the light of the local structural imilarity with TPR-PP5. As we commented in our closing emarks (Bolanos-Garcia et al., 2005, page 2648): “However, he direct participation of lipids in the regulation of any mitotic