Pamela Stanley

Professor Stanley obtained her PhD in the laboratory of Prof. David White, Dept. of Microbiology, University of Melbourne, Australia. She was subsequently a postdoctoral fellow of the MRC of Canada in the laboratory of Dr. Louis Siminovitch at the University of Toronto, where she began her work on the isolation of somatic cell glycosylation mutants. She was appointed Assistant Professor of Cell Biology at Albert Einstein in New York in 1977 and became a full Professor in 1986. She was Program Leader of the Molecular Membrane Biology program of the Albert Einstein Cancer Center from 1988 to 2012. She has been Associate Director for Laboratory Research of the Albert Einstein Cancer Center since 2002. From 1994 to 2007 she directed a NIH T32 graduate student training grant. She currently holds the Horace W. Goldstein Foundation Chair at Albert Einstein. Professor Stanley is an Associate Editor of Glycobiology and on the editorial boards of Scientific Reports and FASEB BioAdvances. Her laboratory is funded by grants from the NIH and she is the recipient of the Karl Meyer Award from the Society for Glycobiology and the IGO award from the International Glycoconjugate Organization. Professor Stanley’s laboratory is focused on identifying roles for mammalian glycans in development, cancer and Notch signaling. Her laboratory has isolated a large panel of Chinese hamster ovary (CHO) glycosylation mutants, characterized them at the biochemical, structural and genetic levels, and used them to identify new aspects of glycan synthesis and functions. The Stanley lab has shown that MGAT1 is essential for spermatogenesis in mammals; that loss of MGAT3 and the bisecting GlcNAc on complex N-glycans, leads to increased tumor burden and metastasis in the MMTV/PyMT mouse model of human breast cancer; revealed key functional roles for O-fucose glycans and the three Fringe enzymes in Notch signaling; shown that deletion of the O-fucosyltransferase POFUT1 leads to embryonic death at mid-gestation with a phenotype typical of global loss of Notch signaling; and that a point mutation to eliminate the O-fucose glycan in the ligand binding domain of NOTCH1 causes defective T cell development in a mixed genetic background, but embryonic lethality in a C57BL/6J background. The Stanley laboratory is currently investigating roles for the O-fucose glycans of NOTCH receptors in T and B cell development and intestinal development and cancer, as well as determining why MGAT1 is required for spermatogenesis, and biological roles of the testis-specific inhibitor of MGAT1 termed MGAT4D.