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Dishevelled localization and function are differentially regulated by structurally distinct sterols.

Sonali Sengupta1, Jazmine D W Yaeger1, Maycie M Schultz1

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Sterols regulate Dishevelled (DVL) protein activity by influencing its membrane binding and localization. Aberrant sterols disrupt DVL signaling, potentially linking sterol metabolism disorders to cellular dysfunction.

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Area of Science:

  • Molecular and Cellular Biology
  • Biochemistry
  • Signal Transduction

Background:

  • The Dishevelled (DVL) protein family is crucial for cellular processes like tissue patterning and polarity.
  • DVL proteins form complexes at the plasma membrane, and cholesterol binding is essential for this association.
  • The precise structural requirements and cellular consequences of DVL-sterol interactions remain largely unknown.

Purpose of the Study:

  • To investigate the role of sterol structure in regulating DVL protein activity.
  • To determine the cellular impacts of DVL-sterol association under normal and pathological conditions.
  • To explore the link between altered sterol homeostasis and DVL signaling pathways.

Main Methods:

  • In silico modeling and molecular analyses to assess DVL-sterol binding.
  • Experiments to evaluate DVL2 plasma membrane association and nuclear localization.
  • Analysis of DVL2 protein-protein interactions and downstream signaling pathway impacts.

Main Results:

  • Sterol orientation within the DVL-PDZ domain dictates binding specificity.
  • Aberrant sterols disrupt DVL2 membrane association, leading to FoxK2-mediated nuclear import.
  • Altered sterol homeostasis selectively impairs DVL2 interactions, affecting multiple signaling cascades.

Conclusions:

  • Sterol specificity is a key regulator of DVL protein signaling.
  • Intracellular sterol levels directly impact DVL localization and functional activity.
  • Aberrant DVL activity may contribute to cellular dysfunction in disorders of sterol metabolism.