Cells remodel actin normally without coronins, challenging textbook view
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.
For decades, textbooks and scientific papers have portrayed coronins as proteins that bind to actin, the primary component of the cytoskeleton. However, a recent study published in PLOS Biology has found that coronins are largely unnecessary for the overall organization of the actin cytoskeleton, contradicting this long-held belief.
Professor Jean Pieters, the lead researcher at the Biozentrum of the University of Basel, and his team examined native coronins using various experimental approaches and discovered that coronin proteins are dispensable for actin binding and remodeling. Despite the absence of evidence for direct actin binding and modulation, cells lacking coronins continue to organize and remodel their actin networks normally.
The researchers also found that tagging coronin proteins with molecular tags, a common practice in biological research, can cause loss of function and alter localization. Additionally, many antibodies used to detect coronins lack specificity, which may have led to false conclusions in previous studies. While the study challenges the traditional view of coronins as cytoskeleton regulators, it does not rule out a connection between coronins and the cytoskeleton.
The researchers suggest that coronins may have key roles in cell signaling, including maintaining normal T-cell numbers, which is crucial for immune system function. By challenging decades-old assumptions, this research may pave the way for new insights into the roles of coronin proteins in signal transduction and cell survival.
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