This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Coronins are found throughout the animal kingdom, from single-celled amoebae to humans, and are involved in many vital processes, including immunity, development and cell survival. For decades, textbooks and hundreds of scientific papers have described coronins primarily as proteins that bind to actin, a key component of the cytoskeleton.
Because of this presumed interaction, coronins have long been regarded as regulators of the cytoskeleton—a network of actin filaments that gives cells their shape, enables them to move and helps organize their contents. But in a new study published in PLOS Biology, researchers led by Professor Jean Pieters at the Biozentrum of the University of Basel challenge this widely accepted view, finding that coronins are largely dispensable for the overall organization of the actin cytoskeleton while demonstrating additional roles for the coronin protein family. In the current study, the researchers comprehensively examined native coronins using a broad range of experimental approaches.
"Over the years, my laboratory failed to find evidence for a direct role of coronin proteins in actin binding and modulation across a wide range of model systems," says Pieters. "Even cells lacking coronins continue to organize and remodel their actin networks normally. Of course, absence of evidence is not evidence of absence." One of the study's most striking results concerns a tool routinely used in biological research.
To visualize and track proteins inside cells, scientists often modify their protein of interest with a molecular tag. "These tags are extremely useful and assumed to be innocuous for protein function," says Roko Gvozdenica, the study's first author. "However, we found that tagging coronin proteins has the potential to cause loss of their function and significantly alter their localization." The researchers assume that at least some of the evidence linking coronins to actin may be plagued by experimental artifacts.
They also found that many antibodies commonly used to detect coronins lack specificity, reinforcing broader concerns about antibody reliability across biomedical research. The researchers point to another function of coronins. "Over the years, we have reported that coronins are involved in cell signaling," emphasizes Pieters.
"In the immune system, for example, coronins' involvement in these signaling processes has been found to be essential for maintaining normal T cell numbers, which is vital for protecting the body against infections or cancer." Although the findings challenge a widely accepted model, they do not rule out a connection between coronins and the cytoskeleton. In fact, coronins may influence how cells organize their cytoskeleton both directly and indirectly through their signaling roles. By revisiting assumptions that have shaped the field for decades, the study may open new avenues for understanding the roles of coronin proteins in signal transduction, including cells' ability to communicate, survive and maintain the delicate balance of cell numbers.
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