Nuclear pore receptor

Expoitins are transport receptors at the nuclear pore complex needed for the selective export of proteins from the nucleus into the cytoplasm. They recognize nuclear export signal sequences of cargo proteins. 

In this chapter we will describe the current understanding of mRNA export. First, we will describe the players in this process, including the nuclear pore, the nuclear pore proteins, and the transport receptors. Then, we will discuss the current understanding of the viral and cellular mRNAs export. Finally, we will discuss current efforts to use the new information on mRNA export to increase the efficiency of transgene expression. 

Erickson, E.S.,Mooren, O.L., Moore-Nichols, D. and Dunn, R.C. (2004)Activation of ryanodine receptors in the nuclear envelope alters the conformation of the nuclear pore complex. Biophys. Chem. 112,1-7. 

A network of intermediate filaments is often found as a laminating layer adjacent to a cellular membrane, where it provides mechanical support. The best example is the nuclear lamina along the inner surface of the nuclear membrane (see Figure 21-16). This supporting network is composed of lamin A and lamin C filaments cross-linked into an orthogonal lattice, which is attached by lamin B to the inner nuclear membrane through interactions with a lamin B receptor, an IFAP, in the membrane. Like the membrane skeleton of the plasma membrane, the lamin nuclear skeleton not only supports the inner nuclear membrane but also provides sites where nuclear pores and interphase chromosomes attach. Thus, the nuclear lamins organize the nuclear contents from the outside in. 

Moore-Nichols, D., A. Amott and R. C. Dunn (2002). "Regulation of nuclear pore complex conformation by ip(3) receptor activation." Biophys 783(3) 1421-8. 

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