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"The PX domain can recognize and interact with a large number of lipid
molecules and other proteins," said Cho. "We study how particular
types of PX domains recognize specific lipids."
In the papers, Cho describes the structure and function PX domains
from two proteins, KIF16B and Bem1p, which interact with a class of
signaling lipids called phosphoinositides.
"KIF16B-PX domain is a critical component of the regulatory mechanism
to modulate the duration of receptor-mediated cell signaling
pathways," Cho said. "That's important because both prolonged and
shortened signaling pathways will cause problems."
"Bem1p-PX domain is a yeast scaffold protein that's critical for cell
polarity. It serves as an excellent model system to study how a
scaffold protein goes to the cell membrane in response to a particular
lipid signal, and then modulates multiple protein-protein interactions."
Cho's research group pioneered a novel biophysical approach to explain
the complex mechanisms by which cellular lipid signals specifically
and divergently activate a wide array of lipid binding domains and the
proteins harboring these domains during various cellular processes.
"This research may help in development of new types of small molecules
and drugs that specifically modulate the signaling and trafficking
processes," Cho said. "For example, if a cellular malfunction is
caused by over-activation of a particular lipid-mediated pathway, then
we can turn off that pathway by developing a compound that interferes
with the interaction of the lipid with its binding protein."
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