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Phosphorylation-dependent structure and dynamics of caveolin-1 8S complex.

Ukesh Karki1, Sadeq Shabani2, Prabin Dahal1

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Phosphorylation of caveolin-1 (Cav-1) at tyrosine 14 alters its N-terminal tail structure, enhancing membrane interactions and regulating caveolae formation. This study reveals Cav-1 phosphorylation as a molecular switch controlling its function.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Caveolin-1 (Cav-1) is a key scaffolding protein involved in membrane dynamics, lipid regulation, and cellular signaling.
  • Phosphorylation at tyrosine 14 (Y14) is known to modulate Cav-1 function, but its structural impact is unclear.
  • The N-terminal tail of Cav-1, crucial for its function, is often unresolved in structural studies.

Purpose of the Study:

  • To investigate the structural consequences of Cav-1 Y14 phosphorylation.
  • To model the full-length human Cav-1 8S complex and its phosphorylated form (pCav-1).
  • To elucidate the role of the N-terminal tail and phosphorylation in Cav-1's membrane interactions and structural dynamics.

Main Methods:

  • Utilized AlphaFold 3 for full-length human Cav-1 8S complex and pCav-1 modeling.
  • Performed molecular dynamics simulations of both complexes within a plasma membrane environment.
  • Analyzed conformational changes and protein-membrane interactions.

Main Results:

  • AlphaFold 3 models incorporating the N-terminal tail revealed significant protein-membrane interactions.
  • Y14 phosphorylation induced substantial conformational alterations in the N-terminal tail.
  • Enhanced inter-protomer hydrogen bonding was observed in the phosphorylated state, leading to an altered conformational state.

Conclusions:

  • Cav-1's N-terminal tail plays a critical role in membrane binding.
  • Y14 phosphorylation acts as a molecular switch, regulating Cav-1's structure, membrane affinity, and caveolae biogenesis.
  • The study provides mechanistic insights into Cav-1 regulation by phosphorylation.