| Functional interaction between BMPR 2 and Tctex 1 , a light chain of Dynein , is isoform specific and disrupted by mutations underlying primary pulmonary hypertension . ^^^ We now report that Tctex 1 , a light chain of the motor complex dynein , interacts with the cytoplasmic domain of BMPR 2 and demonstrate that Tctex 1 is phosphorylated by BMPR 2 , a function disrupted by PPH disease causing mutations within exon 12 . ^^^ Finally we show that BMPR 2 and Tctex 1 co localize to endothelium and smooth muscle within the media of pulmonary arterioles , key sites of vascular remodelling in PPH . ^^^ Taken together , these data demonstrate a discrete function for the cytoplasmic domain of BMPR 2 and justify further investigation of whether the interaction with and phosphorylation of Tctex 1 contributes to the pathogenesis of PPH . . ^^^ |