Abstract
The vertebrate inner nuclear membrane protein, lamin B receptor, has an N-terminal ~200 residue nucleoplasmic domain (NTD), and a ~420 residue C-terminal domain (CTD) that anchors the NTD to the INM. Chen et al (2016) showed the NTD interacts with Xist long noncoding RNA to effect X chromosome inactivation in female mammals. Tsai et al (2016) showed the CTD has sterol reductase activity that is essential for viability. And Nikolakaki et al (2017) proposed a model to interconnect these disparate functions of this chimeric protein. It amuses me now to think back to 24 years ago, when I was concerned that these domains might have come together in a cloning artifact.
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