Researchers Decipher Cellular Code Crucial to Health

Unlocking the secrets of protein folding to combat disease.

Scientists are unraveling a vital cellular “glyco-code,” offering new insights into how proteins properly form within the human body. This groundbreaking research could revolutionize treatments for a range of devastating illnesses, from cystic fibrosis to Alzheimer’s disease.

Unveiling the Glyco-Code

The complex process by which proteins attain their final, functional shape is now better understood, thanks to the work of the late Daniel Hebert, a biochemistry and molecular biology professor at the University of Massachusetts Amherst, and his colleagues. Their findings, published in Nature Reviews Molecular Cell Biology, detail how proteins fold correctly.

Hebert’s research centered on the “glyco-code,” a set of carbohydrate instructions written on the proteins themselves. This code guides the protein folding process.

The ER is an incredibly cluttered and chaotic environment, says Kevin Guay, Hebert’s final graduate student and first author of the new paper. “Dan spent his life detailing how carbohydrate-related chaperones direct the protein folding process and guide proteins to their ultimate locations.”

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“The ER is an incredibly cluttered and chaotic environment,”

—Kevin Guay, Hebert’s Final Graduate Student

Errors in protein production are linked to hundreds of diseases. The National Institutes of Health estimates that misfolded proteins contribute to at least 1,500 genetic disorders (NIH, 2024).

The Role of Chaperones

Special molecules, known as chaperones, assist proteins in folding into their correct shapes. They also identify misfolded proteins. The cell’s quality control department sometimes malfunctions, leading to severe health issues.

Researchers have shown that chaperones use sugar molecules called N-glycans to guide this process. “It’s almost like N-glycans are a postal code using the glyco-code like a home address to deliver a package,” according to Kevin Guay, Hebert’s final graduate student.

Future Implications

The recent publication comprehensively details the mechanics of how proteins are tagged with N-glycans. It also describes how lectins, or chaperones that read the glyco-code, move the proteins to their final locations.

Lila Gierasch, a distinguished professor at UMass Amherst, noted, “Since the placement of the N-glycan now emerges as crucial for the maturation of that specific protein, then continuing Hebert’s work into understanding the whole chaperone system as completely as possible is crucial if we want to treat the diseases that can result from misfolded proteins.”