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Many regulatory mechanisms concerning the translocation of cargo proteins through nuclear pores have been elucidated.
Translocation of cargo proteins by the PA63 pore has been studied extensively in planar lipid bilayer systems.
Binding of ATP re-closes the cleft in a manner that tightly couples to translocation of cargo, via kinesin's 'neck linker' element.
These include roles in cell division [ 20], translocation of cargo along microtubules via dynein [ 21, 22], actin polymerization [ 23], and transcriptional regulation via chromatin/ heterochromatin remodeling [ 24- 26].
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It participates in different protein complexes during the translocation of cargos from the cytosol to the peroxisomal matrix.
The mechanisms governing translocation of cargos by teams of microtubule motors have predominantly been tackled in two ways.
As described in the introduction, there is substantial debate on the influence of total motor copy number on the translocation of cargos.
Karyopherins directly interact with FG-nucleoporins, and somehow this overcomes the gating mechanism and allows translocation of cargoes across the NPC.
These receptors deliver their cargo to the docking complex on the peroxisomal membrane and then participate in the translocation of the cargo across the peroxisomal membrane [ 17].
The neck linker connects the C-terminus of the motor domain to the stalk, so that docking is accompanied by translocation of the cargo and the partner in the direction of travel.
The combined evidence from the cellular ribonucleoprotein particle and viral capsid transport systems makes it likely that vesicle transport represents a general mechanism for translocation of large cargo from the nucleus to the cytoplasm that herpesviruses have usurped during evolution.
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