The study by Cronshaw et al. (2002) provides a comprehensive proteomic analysis of the mammalian nuclear pore complex (NPC), which is crucial for nucleocytoplasmic transport. The authors used mass spectrometry to identify and classify all protein components of a biochemically purified NPC fraction from rat liver nuclei. They identified 29 nucleoporins and 18 NPC-associated proteins, including six previously unknown nucleoporins and a novel family of WD repeat nucleoporins. One of these WD repeat nucleoporins, ALADIN, is associated with triple-A syndrome. The analysis reveals that the mammalian NPC shares a similar number of distinct proteins with its yeast counterpart, suggesting conserved basic functions. However, the vertebrate NPC is larger and more complex, with additional domains and specialized functions, such as mitotic breakdown and interaction with the nuclear lamina. The study also highlights the conservation of certain NPC components between yeast and mammals, indicating that the overall structure and function of the NPC are conserved. The identification of novel nucleoporins and their potential roles in NPC function and disease pathogenesis opens new avenues for further research.The study by Cronshaw et al. (2002) provides a comprehensive proteomic analysis of the mammalian nuclear pore complex (NPC), which is crucial for nucleocytoplasmic transport. The authors used mass spectrometry to identify and classify all protein components of a biochemically purified NPC fraction from rat liver nuclei. They identified 29 nucleoporins and 18 NPC-associated proteins, including six previously unknown nucleoporins and a novel family of WD repeat nucleoporins. One of these WD repeat nucleoporins, ALADIN, is associated with triple-A syndrome. The analysis reveals that the mammalian NPC shares a similar number of distinct proteins with its yeast counterpart, suggesting conserved basic functions. However, the vertebrate NPC is larger and more complex, with additional domains and specialized functions, such as mitotic breakdown and interaction with the nuclear lamina. The study also highlights the conservation of certain NPC components between yeast and mammals, indicating that the overall structure and function of the NPC are conserved. The identification of novel nucleoporins and their potential roles in NPC function and disease pathogenesis opens new avenues for further research.