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A unique IBMPFD-related P97/VCP mutation with differential binding pattern and subcellular localization.

Yalcin Erzurumlu1, Fadime Aydin Kose, Oguz Gozen

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Mutations in p97/VCP cause IBMPFD. The P137L variant uniquely disrupts cofactor binding and localization, offering insights into disease mechanisms.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • p97/VCP (Valosin-containing protein) is a crucial AAA-ATPase involved in protein degradation pathways like ERAD.
  • Mutations in p97/VCP cause the autosomal dominant disorder IBMPFD (Inclusion body myopathy with Paget's disease of the bone and frontotemporal dementia).

Purpose of the Study:

  • To investigate the functional impact of twelve IBMPFD-associated p97/VCP missense mutations on ERAD and cofactor interactions.
  • To characterize the unique properties of the P137L mutant.

Main Methods:

  • Analysis of ERAD substrate accumulation in cells expressing p97/VCP variants.
  • In vitro binding assays to assess interactions with cofactors p47, Ufd1-Npl4, and gp78.
  • Assessment of protein solubility and subcellular localization for the P137L mutant.

Main Results:

  • All twelve p97/VCP mutants caused ERAD substrate accumulation.
  • Most mutants showed enhanced binding to p47 and Ufd1-Npl4.
  • The P137L mutant displayed altered solubility, localization, and a complete loss of binding to Ufd1, Npl4, and p47, while retaining gp78 binding.
  • The R155C mutant retained binding to Ufd1 and gp78 (VIM), unlike P137L.

Conclusions:

  • Differential impairments in p97/VCP interactions with its partners contribute to IBMPFD pathogenesis.
  • The P137L mutation's unique disruption of cofactor binding and cellular behavior provides specific insights into disease mechanisms.