Proteomic analysis of the mammalian nuclear pore complex

By J. Cronshaw, A. Krutchinsky, Wenzhu Zhang, Brian T. Chait, M. Matunis. Journal of Cell Biology, 2002

1,002 citations recorded by the source corpus.

As the sole site of nucleocytoplasmic transport, the nuclear pore complex (NPC) has a vital cellular role. Nonetheless, much remains to be learned about many fundamental aspects of NPC function. To further understand the structure and function of the mammalian NPC, we have completed a proteomic analysis to identify and classify all of its protein components. We used mass spectrometry to identify all proteins present in a biochemically purified NPC fraction. Based on previous characterization, sequence homology, and subcellular localization, 29 of these proteins were classified as nucleoporins, and a further 18 were classified as NPC-associated proteins. Among the 29 nucleoporins were six previously undiscovered nucleoporins and a novel family of WD repeat nucleoporins. One of these WD repeat nucleoporins is ALADIN, the gene mutated in triple-A (or Allgrove) syndrome. Our analysis defines the proteome of the mammalian NPC for the first time and paves the way for a more detailed characterization of NPC structure and function.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/86c735d9469146adb542e3db78a9df3d4241fe43

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In Molecular Biology

1. Michael P. Rout
2. M. Stewart
3. Debashish Chowdhury

Citations in the corpus

• Mechanisms of Receptor‐Mediated Nuclear Import and Nuclear Export (2005, background): “Proteomic characterization of the mammalian and yeast NPC has shown that it comprises approximately 30 proteins (53,54).”
• Molecular mechanism of the nuclear protein import cycle (2007, background): “NPCs are constructed from multiple copies of ∼30 different proteins collectively called nucleoporin”
• The nuclear pore complex: bridging nuclear transport and gene regulation (2010, background): “FG Nups can be classified into two groups: symmetric, which are found on both sides of the NPC (for example NUP62 ), and asymmetric, which are found further from the central plane of the nuclear envelope and have a clear nuclear or cytoplasmic bias (for example NUP153”
• Comprehending crystalline β-carotene accumulation by comparing engineered cell models and the natural carotenoid-rich system of citrus (2011, neutral): “Two years after this yeast NPC proteomics study, Cronshaw et al. (2002) reported the first vertebrate NPC proteomics data.”
• The nuclear pore complex and nuclear transport. (2010, background): “Recent work, mainly in the yeast Saccharomyces cerevisiae and in vertebrates, has begun to elucidate the molecular architecture of the NPC (Rout et al. 2000; Cronshaw et al. 2002; Alber et al. 2007b).”
• 8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI (2022, background): “Each NPC contains approximately 550 proteins in fungi or approximately 1000 proteins in vertebrates (Rout et al., 2000; Cronshaw et al., 2002; Ori et al., 2013).”