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

Mohammad Soheilypour1, Mohaddeseh Peyro1, Hengameh Shams1

  • 1Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, CA, USA.

Nucleus (Austin, Tex.)
|June 3, 2026
PubMed

Insights

Messenger RNA (mRNA) quality control relies on proteins like Myosin-like protein 1 (Mlp1) interacting with RNA-binding proteins (RBPs). This study reveals Mlp1-Nab2 binding involves Nab2

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Nuclear mRNA quality control ensures proper transcript export.
  • Myosin-like protein 1 (Mlp1) interacts with RNA-binding proteins (RBPs) like Nab2.
  • The role of Phe73 in Nab2 for Mlp1 binding is not fully understood.

Purpose of the Study:

  • To elucidate the molecular mechanism of Mlp1-Nab2 interaction.
  • To develop a mechanistic model for Mlp1-Nab2 binding using computational approaches.

Main Methods:

  • Computational modeling to analyze Mlp1-Nab2 interactions.
  • Investigating the impact of Nab2 Phe73 mutations (F73A, F73W) on binding.

Main Results:

  • Nab2's Phe73 stabilizes intramolecular helix interactions, promoting a compact conformation, rather than direct Mlp1 contact.
  • Mutation F73A weakened Mlp1-Nab2 binding by disrupting helix stabilization.
  • Mutation F73W enhanced Mlp1-Nab2 interaction.

Conclusions:

  • Mlp1-Nab2 binding is mediated by Nab2's structural flexibility and Mlp1's disordered domain.
  • This adaptive recognition mechanism is crucial for mRNA quality control by the nuclear basket.
  • Flexible protein-protein recognition is vital for nuclear mRNA surveillance.
Keywords:
RNA-binding proteins (RBPs)intrinsically disordered proteinsmRNA exportmRNA quality controlmolecular dynamics simulationsnuclear basketnuclear pore complex (NPC)

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