Cell type-specific nuclear pores: a case in point for context-dependent 
stoichiometry of molecular machines

Ori, Alessandro; Banterle, Niccolò; Iskar, Murat; Andrés-Pons, Amparo; Escher, Claudia; Khanh Bui, Huy; Sparks, Lenore; Solis-Mezarino, Victor; Rinner, Oliver; Bork, Peer; Lemke, Edward A.; Beck, Martin

doi:10.1038/msb.2013.4

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Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines

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Ori, A., Banterle, N., Iskar, M., Andrés-Pons, A., Escher, C., Khanh Bui, H., et al. (2013). Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines. Molecular Systems Biology, 9: 648. doi:10.1038/msb.2013.4.

Cite as: https://hdl.handle.net/21.11116/0000-0006-EACC-D

Abstract

To understand the structure and function of large molecular machines, accurate knowledge of their stoichiometry is essential. In this study, we developed an integrated targeted proteomics and super-resolution microscopy approach to determine the absolute stoichiometry of the human nuclear pore complex (NPC), possibly the largest eukaryotic protein complex. We show that the human NPC has a previously unanticipated stoichiometry that varies across cancer cell types, tissues and in disease. Using large-scale proteomics, we provide evidence that more than one third of the known, well-defined nuclear protein complexes display a similar cell type-specific variation of their subunit stoichiometry. Our data point to compositional rearrangement as a widespread mechanism for adapting the functions of molecular machines toward cell type-specific constraints and context-dependent needs, and highlight the need of deeper investigation of such structural variants.