Karyopherin-mediated import of integral inner nuclear membrane proteins

Article Abstract:

Integral inner nuclear membrane (INM) proteins in cells are confirmed to possess basic sequence motifs resembling 'classical' nuclear localization signals, which mediate direct binding to karyopherin-alpha and are essential for the passage of integral membrane proteins to the INM. Also, karyopherin-alpha, karyopherin-beta1, and the Ran GTPase cycle are required for INM targeting, indicating similarities between mechanisms governing INM targeting and soluble nuclear transport.

Gene mutations, Gene mutation

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Taking a turn into the nucleus

Article Abstract:

Studies reveal that the transmembrane proteins in yeast get into the inner nuclear membrane (INM) by a receptor-mediated transport mechanism. The identification of the classical nuclear localization signal-like sequences in INM proteins lead to the conclusion that transport receptors for soluble proteins called kap-alpha/beta1 also facilitate the passage of membrane proteins through nuclear pore complexes.

Cell nuclei, Cell nucleus

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Pore puzzle

Article Abstract:

The biochemical and morphological data results, which provide insight into, yeast nuclear pore complexes (NPCs) structure and assembly is presented.

Glycine, Phenylalanine, Structure

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