Actin-Binding Proteins in the Nucleolus During Heat Shock
Author Information
Author(s): Taniguchi Shinya, Torii Takeru, Goto Toshiyuki, Takeuchi Kohei, Katsumi Rine, Sumida Mako, Lee Sunmin, Sugimoto Wataru, Gessho Masaya, Itoh Katsuhiko, Hirata Hiroaki, Kawakami Junji, Miyoshi Daisuke, Kawauchi Keiko
Primary Institution: Faculty of Frontiers of Innovative Research in Science and Technology (FIRST), Konan University
Hypothesis
Nucleolar actin-binding proteins might be sequestered during heat shock to prevent irreversible aggregation.
Conclusion
The study identifies 10 actin-binding proteins with high levels of intrinsically disordered regions that may play a role in the heat shock response.
Supporting Evidence
- Heat shock induces the reversible assembly of nAC-GFP in the nucleolus.
- 47 actin-binding proteins were identified to localize in the nucleolus.
- 10 of these proteins exhibited high levels of intrinsically disordered regions.
- PDLIM7 and TRIOBP were highlighted for their increased expression in response to heat shock.
Takeaway
When cells get too hot, a special part inside them called the nucleolus helps keep proteins from getting messed up by using actin, a building block of cells.
Methodology
The study used a GFP-tagged actin chromobody to visualize nuclear actin dynamics in HeLa cells during heat shock and performed bioinformatic analyses to identify actin-binding proteins.
Digital Object Identifier (DOI)
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