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Engineered tagged Profilin-1 (PFN1) proteins enable studying its function in cell processes. These tools revealed PFN1 interactions with actin and microtubules, crucial for cell morphology and division.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Profilin-1 (PFN1) is a key cytoskeletal protein regulating actin and microtubule dynamics, essential for cell division, motility, and morphology.
  • Conventional protein tagging methods often interfere with PFN1's native functions, limiting in vivo studies.
  • Previous PFN1 research relied on indirect methods and cell-free assays.

Purpose of the Study:

  • To engineer and characterize genetically encoded, functional tagged versions of Profilin-1 (PFN1).
  • To utilize these tagged PFN1 proteins to investigate its interactions with actin and microtubules in live cells.
  • To explore the role of PFN1 in cellular functions and disease states, such as ALS.

Main Methods:

  • Engineered two genetically encoded tagged PFN1 variants (Halo-PFN1, mApple-PFN1) exhibiting identical behavior to tag-free PFN1.
  • Performed biochemical assays to assess PFN1's interaction with phosphoinositide lipids, actin monomers, and tubulin dimers.
  • Utilized self-labeling Halo-ligands and function-disrupting mutants in PFN1-deficient mammalian cells for live-cell imaging and functional rescue experiments.

Main Results:

  • Purified tagged PFN1 proteins demonstrated biochemical activities including actin nucleotide exchange and stimulation of formin-mediated actin assembly.
  • Tagged PFN1 variants restored normal morphology and cytoskeletal functions in PFN1-deficient cells.
  • Live-cell imaging revealed PFN1 binding to microtubules and demonstrated that the ALS-associated G118V variant failed to associate with actin or microtubules.

Conclusions:

  • Genetically encoded tagged PFN1 proteins are reliable tools for studying PFN1 dynamics and interactions in vitro and in vivo.
  • These tools facilitate the investigation of PFN1's role in cellular processes and disease pathogenesis.
  • The study provides new insights into PFN1's interaction with microtubules and the functional consequences of disease-associated mutations.