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Esgleas Izquierdo, M. ; Falk, S. ; Forné, I.* ; Thiry, M.* ; Najas, S. ; Zhang, S.* ; Mas-Sanchez, A. ; Geerlof, A. ; Niessing, D. ; Wang, Z.* ; Imhof, A.* ; Götz, M.

Trnp1 organizes diverse nuclear membrane-less compartments in neural stem cells.

EMBO J.:e103373 (2020)
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Open Access Gold (Paid Option)
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TMF1-regulated nuclear protein 1 (Trnp1) has been shown to exert potent roles in neural development affecting neural stem cell self-renewal and brain folding, but its molecular function in the nucleus is still unknown. Here, we show that Trnp1 is a low complexity protein with the capacity to phase separate. Trnp1 interacts with factors located in several nuclear membrane-less organelles, the nucleolus, nuclear speckles, and condensed chromatin. Importantly, Trnp1 co-regulates the architecture and function of these nuclear compartmentsin vitroand in the developing brainin vivo. Deletion of a highly conserved region in the N-terminal intrinsic disordered region abolishes the capacity of Trnp1 to regulate nucleoli and heterochromatin size, proliferation, and M-phase length; decreases the capacity to phase separate; and abrogates most of Trnp1 protein interactions. Thus, we identified Trnp1 as a novel regulator of several nuclear membrane-less compartments, a function important to maintain cells in a self-renewing proliferative state.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Heterochromatin ; Mitosis ; Nuclear Speckles ; Nucleolus ; Phase-transition; Phase-separation; Ribosome Biogenesis; Intrinsic Disorder; Proteins; Rna; Cycle; Transcription; Nucleolus; Domains; Complex
ISSN (print) / ISBN 0261-4189
e-ISSN 1460-2075
Quellenangaben Volume: , Issue: , Pages: , Article Number: e103373 Supplement: ,
Publisher Wiley
Publishing Place Heidelberg, Germany
Reviewing status Peer reviewed