Work in the nuclear transport field has led to an incredibly detailed description of protein translocation through the central channel of the nuclear pore complex, yet the mechanism by which nuclear envelope transmembrane proteins reach the inner nuclear membrane after synthesis in the endoplasmic reticulum is still hotly debated. Three different translocation models have gained experimental support: (i) simple lateral diffusion through the nuclear envelope membrane system; (ii) translocation by vesicle fusion events; and (iii) a variation on classical transport mediated by the nuclear pore complex. Although these models appear to be mutually exclusive, in the present paper we argue that they probably all function for different inner nuclear membrane proteins according to their unique characteristics.

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