Tiny "blob-like" proteins that move around and disappear within cells; researchers are still not sure of the purpose of these structures, but the "cloud-like" collection could be offer new developments in disease treatment.
The researchers highlighted the need to study these structures, recently dubbed "assemblages," Georgetown University Medical Center reported.
"I want to know what these assemblages are doing in Ewing sarcoma, the disease I concentrate on - and I would think all other researchers who study human biology would want to know their functions in both health and disease," said Jeffrey Toretsky, MD, professor in the department of oncology and pediatrics at Georgetown Lombardi Comprehensive Cancer Center.
Researchers pooled their biophysics and protein biochemistry knowledge on assemblages in order to put together a review.
The researchers believe these proteins are usually (but not always) made up of proteins that are intrinsically disordered, meaning they do not take on a specific shape in order to fit "like a lock" into other proteins. The proteins tend to form themselves into gel-like assemblages in a process called "phase separation," which can trap and interact with other proteins and RNA, which "decode and regulate" genes.
"It is only in the last five years that researchers have begun recognizing that proteins without fixed structures may have important transitional properties that change based upon their local abundance in cells," Toretsky said.
The researcher suggests these assemblages are crucial to cell health, and therefore could play a role in disease treatment.
"Current drug-discovery dogma suggests that it is very hard to make a small molecule to prevent two structured proteins from interacting. However, small molecules have a greater likelihood of disrupting intrinsically disordered protein-protein interactions," Toretsky said.
"This review links together very basic biologic phenomena of protein interaction with the potential for new drug discovery," Toretsky says. "It's an exciting challenge."
The findings were published in a recent edition of the Journal of Cell Biology; co-author Peter Wright, PhD, professor in the department of integrative structural and computational biology at The Scripps Research Institute also worked on the study.
