Felix T. Wieland (born 1948) is a German biochemist and a senior professor at Heidelberg University. He served as president of the German Society for Biochemistry and Molecular Biology from 2005 to 2007 and was managing editor of the journal FEBS Letters from 2001 to 2021.
Wieland's research concerned the transport of proteins between cell compartments, the analysis of membrane lipids, and the interactions of lipids with proteins. He is an elected member of the German National Academy of Sciences Leopoldina, the European Molecular Biology Organization and the Academia Europaea.
Early life and education Wieland was born in 1948. He is a grandson of Heinrich Wieland and a nephew of Feodor Lynen and of Theodor Wieland.
He studied chemistry at LMU Munich from 1969 to 1975. Afterwards, he carried out doctoral research at the Max Planck Institute of Biochemistry in Martinsried under Lynen between 1975 and 1978.
Career Wieland moved to the University of Regensburg in 1978. There he held academic posts until 1986 and completed his habilitation in 1984. After meeting James Rothman in 1985, he spent a sabbatical in Rothman's laboratory at Stanford University from 1986 to 1988, working on the mechanisms of intracellular transport.
In 1988, he became a professor at Heidelberg University's Medical Faculty, and held the professorship until 2018, when he was appointed a senior professor of the university.
Wieland joined the editorial board of FEBS Letters in 1994 and was its managing editor from 2001 to 2021. He was president of the German Society for Biochemistry and Molecular Biology from 2005 to 2007.
Research In his early career, Wieland studied the relative arrangement of the two subunits of yeast fatty acid synthase, which is a large multienzyme complex, by combining antibody crosslinking with negative stain electron microscopy. Using this approach, he developed a three-dimensional model of the enzyme in 1978.
At Regensburg, Wieland worked with Manfred Sumper and Josef Lechner on the cell surface glycoprotein of the archaeon Halobacterium salinarum. Through the 1980s he and his colleagues reported the structures of its glycans and aspects of their biosynthesis, sequenced a gene encoding a glycosylated archaeal surface layer protein, and found that glycosylation determines the shape of the cells. In 1985, with Gerhard Paul and Sumper, he showed that the organism's flagellins are glycoproteins.
Working with James Rothman, Wieland measured the rate of bulk flow of newly made protein from the endoplasmic reticulum to the cell surface. Their laboratories developed the budding assay in which purified Golgi membranes and cytosol generate coated vesicles. Afterwards, his work focused on the COPI coat, which packages proteins into vesicles for transport between the Golgi apparatus and the endoplasmic reticulum. In 1999 he reported the reconstitution of COPI vesicle budding from a minimal set of purified components. Later with John Briggs, he produced a molecular model of the coat by using reconstituted vesicles.
Wieland, Britta Brügger, and Wolf-Dieter Lehmann developed a nano-electrospray mass spectrometric method for quantifying membrane lipids at low picomole amounts. Wieland and Brügger also examined how proteins and lipids interact in membranes, and, in 2012, reported that a single molecule of one specific species of sphingomyelin binds the transmembrane domain of the p24 coat subunit and regulates formation of the COPI coat.
Awards 2000 - Elected member, European Molecular Biology Organization 2001 - Heinrich Wieland Prize, Boehringer Ingelheim Stiftung 2003 - Elected member, Leopoldina 2006 - Feldberg Foundation Prize 2011 - Elected member, Academia Europaea
Selected publications
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