The inner nuclear membrane (INM) accommodates a specific set of integral membrane proteins many of which interact with chromatin and/or in metazoan cells with the lamina network. The localization of these proteins characterizes this membrane area of the nuclear envelope (NE) despite the fact that the INM forms a membrane continuum with the outer nuclear membrane (ONM) and the remaining endoplasmic reticulum (ER). In fact, the INM can be regarded as a highly specialized membrane subdomain of the ER. How the specific protein composition of the INM is established and maintained and whether this is achieved via a single unifying mechanism is by and large unclear. Recent experiments shed light on some aspects of the process.
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Antonin et al. (2011) studied this question.
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