The metazoan nuclear envelope needs to be rapidly re-assembled around de-condensing chromatin at the end of cell division. As little is known about the mechanisms responsible for coordinating chromatin remodelling with membrane reconstruction, Wolfram Antonin and colleagues set out to perform a screen for inhibitors of nuclear envelope assembly. In their work (p. 3466), they describe a new role for the lysine-specific histone demethylase 1 (LSD1) in nuclear membrane formation. They showed that chemical inhibition or depletion of LSD1 prevented nuclear re-assembly in an in vitro assay with Xenopus laevis egg extracts. Using HeLa cells, the authors then observed that cells in which LSD1 was knocked down had a decreased nuclear volume; these cells also spent significantly longer in telophase and chromatin de-condensation was delayed. Although LSD1 depletion did not affect nuclear lamina assembly, it caused defects in the re-assembly of nuclear pore complexes (NPCs). Notably, although LSD1 was not required for chromatin de-condensation, its depletion prevented the recruitment of membrane to chromatin extracted from HeLa cells. Finally, as shown here, the demethylase activity of LSD1 was required for recruitment of chromatin-binding membrane fractions that contain transmembrane nucleoporins, and of MEL28, which is needed for the initiation of NPC assembly. Thus, this study is the first demonstration that LSD1 has a role in chromatin-dependent membrane recruitment and is necessary for efficient nuclear envelope assembly at the end of mitosis.