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D6PKL3 is a membrane-associated protein kinase that premarks distinct membrane microdomains during pollen aperture formation

Research Scholar

Byungha Lee, post-doctoral researcher, Kyungpook National University (South Korea)
Anna A. Dobritsa, Faculty Mentor


  • Hometown: South Korea
  • Degrees received: PhD in plant molecular biology, Kyungpook National University, South Korea.

What is the issue or problem addresses in your research?

Exine is deposited on the surface of pollen at specific positions and assembles into intricate 3-dimensional patterns, though the mechanism is not fully understood. Areas of limited exine deposition are called apertures. INP1 was the only known protein involved in aperture formation. Interested in identifying and characterizing others, we concluded that D6PKL3 is a novel, essential player in aperture formation in Arabidopsis pollen.

What methodology did you use in your research?

I used yeast two-hybrid (Y2H), biomolecular fluorescence complementation (BiFC) for checking interaction between INP1 and D6PKL3. I used a protein-lipid binding assay for understanding how those two proteins, INP1 and D6PKL3, bind to the pollen surface area. I analyzed localization of INP1 and D6PKL3 during pollen development using confocal microscopy.

What are the purpose/rationale and implications of your research?

We seek better characterize pollen aperture formation. Our look into D6PKL3 indicates that it may indirectly guide INP1 to the pollen surface, though more proteins are probably involved in this process since localization is temporally distant, though spatially similar, and direct protein-protein interactions were not detected.