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<p>p47/NSFL1C is a key adaptor protein of p97/VCP, a AAA+ ATPase that is involved in a diverse array of cellular functions. p47 directs p97 activity towards membrane remodelling and contributes to the regulation of cellular pathways such as NF-κB signalling and autophagy. p47 consists of three folded domains (UBA, SEP, UBX) connected by extended intrinsically disordered regions (IDRs). The dynamic and flexible nature of p47 has hindered high-resolution structural characterization of the full-length protein and its complex with p97 by X-ray crystallography or cryo-EM. Here, we report NMR backbone resonance assignments and secondary structure propensities of full-length p47, as well as of a truncated construct containing a SEP-interacting motif (SIM) and the SEP domain (residues 101–266). These findings provide the basis for future NMR studies aimed at elucidating the structural mechanisms by which p47 regulates p97 activity and for rational design of molecular binders to selectively target p47 and modulate specific p47-dependent pathways.</p>

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1H, 13C, and 15N backbone resonance assignments of full-length and a SIM-SEP-containing fragment (101–266) of p47, a p97 adaptor protein

  • 期刊论文

  • 发表日期：

    2025年11月5日

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  • Rajivan Raseekan,
  • Megan K. Black,
  • Rui Huang

摘要

p47/NSFL1C is a key adaptor protein of p97/VCP, a AAA+ ATPase that is involved in a diverse array of cellular functions. p47 directs p97 activity towards membrane remodelling and contributes to the regulation of cellular pathways such as NF-κB signalling and autophagy. p47 consists of three folded domains (UBA, SEP, UBX) connected by extended intrinsically disordered regions (IDRs). The dynamic and flexible nature of p47 has hindered high-resolution structural characterization of the full-length protein and its complex with p97 by X-ray crystallography or cryo-EM. Here, we report NMR backbone resonance assignments and secondary structure propensities of full-length p47, as well as of a truncated construct containing a SEP-interacting motif (SIM) and the SEP domain (residues 101–266). These findings provide the basis for future NMR studies aimed at elucidating the structural mechanisms by which p47 regulates p97 activity and for rational design of molecular binders to selectively target p47 and modulate specific p47-dependent pathways.