Intrinsically disordered regions facilitate Mlp1-Nab2 recognition in mRNA quality control.

Mohammad Soheilypour, Mohaddeseh Peyro, Hengameh Shams, Mohammad R K Mofrad

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In one paragraph

Article in Nucleus (Austin, Tex.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Mohammad SoheilypourMolecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, CA, USA.

Mohaddeseh PeyroMolecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, CA, USA.

Hengameh ShamsMolecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, CA, USA.

Mohammad R K MofradMolecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, CA, USA.ORCID 0000-0001-7004-4859

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Quality control of mRNAs ensures that only properly processed transcripts are exported from the nucleus. Myosin-like protein 1 (Mlp1), plays a central role in this process by interacting with RNA-binding proteins (RBPs), including Nab2. While previous studies identified Phe73 in Nab2 as critical for Mlp1 binding, the molecular mechanism remains unclear. Here, we employed a computational approach to develop a mechanistic model of Mlp1-Nab2 interaction. Our results suggest that Phe73 does not act through direct contacts with Mlp1, but instead stabilizes intramolecular interactions between Nab2 helices that promote a compact conformation. F73A disrupted this helix-helix stabilization and weakened binding, whereas F73W enhanced the interaction. Our findings support a binding mechanism in which the structural flexibility of Mlp1's disordered domain enables adaptive recognition of Nab2. This mechanism may represent a general strategy by which the nuclear basket inspects mRNPs, highlighting the importance of flexible protein-protein recognition in mRNA quality control.

Indexed as

Intrinsically Disordered ProteinsRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsNucleocytoplasmic Transport ProteinsProtein BindingIntrinsically Disordered ProteinsNAB2 protein, S cerevisiaeNucleocytoplasmic Transport ProteinsRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae Proteinsintrinsically disordered proteinsmolecular dynamics simulationsmRNA exportmRNA quality controlnuclear basketnuclear pore complex (NPC)RNA-binding proteins (RBPs)

Identifiers

PMID42233425

DOI10.1080/19491034.2026.2680376

PMCPMC13240961

What Socratic holds

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LicenceCC BY

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.