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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.
Mol Syst Biol ; 9: 648, 2013.
Artigo em Inglês | MEDLINE | ID: mdl-23511206
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.