The evolutionarily conserved deubiquitinase UBH1/UCH-L1 augments DAF7/TGF-β signaling, inhibits dauer larva formation, and enhances lung tumorigenesis.

Modification of the transforming growth factor β (TGF-β) signaling components by (de)ubiquitination is emerging as a key regulatory mechanism that controls cell signaling responses in health and disease. Here, we show that the deubiquitinating enzyme UBH-1 in and its human homolog, ubiquitin C-terminal hydrolase-L1 (UCH-L1), stimulate DAF-7/TGF-β signaling, suggesting that this mode of regulation of TGF-β signaling is conserved across animal species. The dauer larva-constitutive phenotype caused by defective DAF-7/TGF-β signaling was enhanced and suppressed, respectively, by deletion and overexpression in the loss-of-function genetic backgrounds of , /TGF-βRI, and /R-SMAD, but not of /R-SMAD.

Rhodium(I)-Catalyzed Ring-Closing Reaction of Allene-Alkene-Alkynes: One-Step Construction of Tricyclo[6.4.0.0 ] and Bicyclo[6.3.0] Skeletons from Linear Carbon Chains.

Treatment of dodecatrienyne derivatives with [RhCl(CO) ] in refluxing toluene effected the cycloisomerization to produce tricyclo[6.4.0.

Characterization of ciliary targeting sequence of rat melanin-concentrating hormone receptor 1.

Melanin-concentrating hormone (MCH) is the natural peptide ligand for MCHR1 and MCHR2, which belong to the G protein-coupled receptor (GPCR) superfamily. The MCH-MCHR1 system is involved in the regulation of feeding, energy homeostasis and emotional processing in rodents. Recently, MCHR1 expression was discovered in neuronal immotile primary cilia of the central nervous system in mice.