Compositional adaptability in NPM1-SURF6 scaffolding networks enabled by dynamic switching of phase separation mechanisms

Mylene C. Ferrolino, Diana M. Mitrea, J. Robert Michael and Richard W. Kriwacki ()
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Mylene C. Ferrolino: St. Jude Children’s Research Hospital
Diana M. Mitrea: St. Jude Children’s Research Hospital
J. Robert Michael: St. Jude Children’s Research Hospital
Richard W. Kriwacki: St. Jude Children’s Research Hospital

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract The nucleolus, the site for ribosome biogenesis contains hundreds of proteins and several types of RNA. The functions of many non-ribosomal nucleolar proteins are poorly understood, including Surfeit locus protein 6 (SURF6), an essential disordered protein with roles in ribosome biogenesis and cell proliferation. SURF6 co-localizes with Nucleophosmin (NPM1), a highly abundant protein that mediates the liquid-like features of the granular component region of the nucleolus through phase separation. Here, we show that electrostatically-driven interactions between disordered regions of NPM1 and SURF6 drive liquid-liquid phase separation. We demonstrate that co-existing heterotypic (NPM1-SURF6) and homotypic (NPM1-NPM1) scaffolding interactions within NPM1-SURF6 liquid-phase droplets dynamically and seamlessly interconvert in response to variations in molecular crowding and protein concentrations. We propose a mechanism wherein NPM1-dependent nucleolar scaffolds are modulated by non-ribosomal proteins through active rearrangements of interaction networks that can possibly contribute to the directionality of ribosomal biogenesis within the liquid-like nucleolus.

Date: 2018
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DOI: 10.1038/s41467-018-07530-1

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