Emerin is a conserved nuclear membrane protein and forms part of nuclear lamina structure. Mutations in nuclear lamina proteins result in a number of diseases, including cardiomyopathy and muscular dystrophy, through unknown mechanisms. The exact molecular role of emerin remains unclear owing to functional overlap with other nuclear membrane proteins and direct interactions with lamins. In this work (p. 3956), Katherine Wilson and colleagues discovered that emerin undergoes intermolecular association in vitro through two modes; one involving amino acids 170–220 in both emerin molecules, and the other involving 170–220 of the first and 1–132 of the second emerin molecule. The authors then employ overexpression of deletion mutants in HEK293T cells to show that part of the association domain (residues 186–220; the ‘R’ region) is essential for emerin intermolecular association. Interestingly, residues 168–186 (the ‘A’ region) were required to restrain emerin–emerin interactions in HeLa cells, suggesting they might inhibit or control the intermolecular association of emerin in vivo. On the basis of these and other results, the authors propose a model in which the R regions of multiple emerins can associate with each other, with another region comprising residues 147–174 (‘S’) or with the LEM domain, to give rise to an emerin network at the nuclear lamina that could be reorganised in response to mechanical force as the basis for mechanotransduction.