Nobel laureates to open ASBMB annual meeting in San Diego

Main Category: Biology / Biochemistry
Article Date: 12 Mar 2005 - 0:00 PDT

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In a first for the American Society for Biochemistry and Molecular Biology (ASBMB), two Nobel Laureates will share the Herbert Tabor/Journal of Biological Chemistry Lectureship. Both Dr. Michael S. Brown and Dr. Joseph L. Goldstein, who were awarded the 1985 Nobel Prize in Physiology or Medicine for their discoveries concerning the regulation of cholesterol metabolism, will be on stage to open the Society's Annual Meeting on April 2 at 6:00 p.m. in San Diego.

The Herbert Tabor/Journal of Biological Chemistry Lecture is the opening lecture of every ASBMB Annual Meeting. The award honors Dr. Tabor for his long service to the Society and to the Journal of Biological Chemistry. Recipients are selected from among those whose names represent outstanding research in addition to service to the Society, including its publication efforts. The Award was instituted in 2004 and the first recipient was Dr. Robert Lefkowitz, James B. Duke Professor and Howard Hughes Medical Institute Investigator at Duke University Medical Center.

Dr. Brown and Dr. Goldstein's lecture will focus on the regulated intramembrane proteolysis (RIP) of sterol regulatory element binding proteins (SREBPs). Materials relating to the lecture will be posted on the ASBMB website (http://www.asbmb.org).

RIP is the process by which membrane-bound proteins are cleaved and fragments are released into the cell's cytosol. These fragments often activate gene transcription. Conserved from bacteria to humans, RIP regulates processes from spore formation to cell differentiation to lipid biosynthesis. Pathologically, it creates the amyloid peptides of Alzheimer's disease.

The Goldstein and Brown laboratory uncovered RIP through study of SREBPs, transcription factors that regulate the synthesis and uptake of cholesterol and fatty acids in animal cells. SREBPs are synthesized as transmembrane proteins. One of the ends of the protein is a transcription factor that projects into the cytosol and is cleaved by RIP. By modulating the processing of SREBPs, RIP directly controls membrane lipid composition and indirectly controls plasma cholesterol levels.

Dr. Goldstein and Dr. Brown have worked together for the last 30 years on the genetics and regulation of cholesterol metabolism. Their discovery of the LDL receptor as the major molecule regulating cholesterol metabolism and its genetic disruption in the human disease familial hypercholesterolemia have been recognized by their receipt of numerous awards, including the Albert D. Lasker Award in Basic Medical Research (1985), the Nobel Prize in Physiology or Medicine (1985), and the U.S. National Medal of Science (1988). More recently, their discovery of the SREBP family of membrane-bound transcription factors and the elucidation of the proteolytic pathway by which the SREBPs become activated to regulate lipid metabolism were recognized by the receipt of the Albany Medical Prize in Biomedical Sciences in 2003.

The American Society for Biochemistry and Molecular Biology is a nonprofit scientific and educational organization with 12,000 members in the United States and internationally. Most members teach and conduct research at colleges and universities. Others conduct research in various government laboratories, nonprofit research institutions, and industry.

Founded in 1906, the Society is based in Bethesda, Maryland, on the campus of the Federation of American Societies for Experimental Biology. The Society's primary purpose is to advance the sciences of biochemistry and molecular biology through its publications, The Journal of Biological Chemistry, Journal of Lipid Research, Molecular and Cellular Proteomics, and Biochemistry and Molecular Biology Education, and the holding of scientific meetings.

For more information about ASBMB see our website: http://www.asbmb.org.

Contact: Nicole Kresge
nkresge@asbmb.org
301-634-7415
American Society for Biochemistry and Molecular Biology
http://www.asbmb.org

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