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Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex.

Amber Vogel1, Alexandra Crawford1, Afua Nyarko1

  • 1Department of Biochemistry & Biophysics, Oregon State University, Corvallis, Oregon, USA.

Protein Science : a Publication of the Protein Society
|April 28, 2022
PubMed
Summary

Researchers studied how cancer-promoting Yes-associated protein (YAP) binds Angiomotin-like 1 (AMOTL1). They found transient interactions fine-tune complex stability, crucial for regulating cell proliferation and potential cancer therapies.

Keywords:
AngiomotinPPxYWW domainYes-associated proteincircular dichroism (CD)intrinsically disordered proteinisothermal titration calorimetry (ITC)multivalentnuclear magnetic resonance spectroscopy (NMR)protein-protein interactionscaffolding protein

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Cancer Research

Background:

  • Yes-associated protein (YAP) is a cancer-promoting co-activator.
  • YAP forms multivalent complexes with PPxY motif proteins, influencing cell proliferation.
  • Understanding YAP-PPxY complex assembly is limited by challenges in producing full-length binding domains.

Purpose of the Study:

  • To produce a functional polypeptide of Angiomotin-like 1 (AMOTL1) containing all three PPxY binding sites.
  • To investigate the biophysical mechanisms of YAP-AMOTL1 complex formation.
  • To elucidate how these interactions regulate YAP nucleo-cytoplasmic shuttling.

Main Methods:

  • Production of a recombinant AMOTL1 polypeptide with three PPxY motifs.
  • Biophysical characterization using isothermal titration calorimetry (ITC).
  • Size-exclusion chromatography coupled to multi-angle light scattering (SEC-MALS).
  • Solution nuclear magnetic resonance (NMR) spectroscopy.

Main Results:

  • The AMOTL1 polypeptide is partially disordered.
  • AMOTL1 binds YAP WW domains, forming an ensemble of complexes with varying stabilities.
  • Binding involves sequential and transient interactions between YAP WW domains and AMOTL1 PPxY motifs.
  • A dynamic equilibrium of complexes with two YAP sites bound to two AMOTL1 sites is formed.

Conclusions:

  • Transient interactions are key to the rapid assembly and disassembly of YAP-AMOTL1 complexes.
  • This dynamic regulation fine-tunes complex stability in response to cellular environment.
  • Findings provide insights into YAP regulation and potential therapeutic strategies targeting cancer proliferation.