Madhura Kulkarni, a UMBI graduate student, and her mentor, Dr. Harold Smith, have published a featured cover story in the July issue of PLoS Genetics, which can be accessed here.

			A fluorescence micrograph of the reproductive tract of the roundworm, C. elegans, bearing a mutation that blocks the attachment of ubiquitin to proteins, visualized by green fluorescent protein. From Kulkarni and Smith.

Proteins are the basic building blocks of biology, and must be produced at the proper time and place in the body to carry out their functions. Equally important, these proteins must be disposed of when they are damaged or no longer needed. The failure to destroy proteins in a timely manner can have serious health consequences: neurodegenerative disorders such as Alzheimer's and Parkinson's diseases are believed to result from the inappropriate accumulation of proteins that are normally degraded.

A recent discovery by researchers at UMBI's Center for Advanced Research in Biotechnology provides insight into the mechanisms of protein degradation. Proteins are targeted for destruction by the attachment of a tag known as ubiquitin. Using the simple roundworm C. elegans as a model for investigation, graduate student Madhura Kulkarni and her advisor Harold Smith have identified a mutation that blocks the attachment of ubiquitin to target proteins, thereby preventing their destruction. This mutation leads to a variety of developmental defects, including growth arrest, reduced body size, and sperm infertility. It also produces progressive paralysis in males, which offers an exciting new animal model for the study of neurodegenerative disorders. "This discovery highlights the importance of using model organisms like C. elegans to understand fundamental biological processes that underlie human disease," said Dr. Smith.