Postdoctoral Training under Dr. Günter Blobel, Laboratory of Cell Biology, Rockefeller University, NY, NY. Ph.D., Department of Molecular Pharmacology, Albert Einstein College of Medicine, Yeshiva University, Bronx, NY. Master of Science. Roswell Park Cancer Institute, Buffalo, NY. Bachelor of Science. Major: Biology. State University of New York at Buffalo, NY. Honors & Awards Harvey N. Davis, Distinguished Teaching Assistant Professor

The long-range goal of the Glavy Lab is to outline the molecular mechanisms of the mitotic breakdown of the nuclear pore complex (NPC) with a main focus on the effects of cell cycle dependent modifications on the regulation of nucleoporins (starting with the Nup107-160 subcomplex) and hence the NPC.

The NPC is the principal passageway for nucleocytoplasmic macromolecular traffic. It is composed of about 30 proteins, termed nucleoporins (Nups) designated by their molecular weights in kilodaltons. These are organized into a pseudo-symmetric structure with a two-fold plane quasi-parallel to the nuclear envelope and an eight-fold axis of symmetry across the nucleo-cytoplasmic axis. Most of the Nups are part of a symmetric core structure and therefore occur in at least 16 copies per NPC (e.g. Nup107, Nup133). Others are present only on either the cytoplasmic or the nucleoplasmic side and are present in eight copies per NPC (e.g. Nup358, Nup214, Nup153 also designated FG Nups because of their regional FG (Phe-Gly) sequence repeats). FG Nups are targets of at least nine chromosomal rearrangements found in leukemia, primarily in acute myelogenous leukemia (AML) and myelodysplastic syndrome (MDS). These chromosomal translocations further effect other related Nups, such as Nup107 and Nup133, demonstrating their interdependence which is critical during cell division.

The NPC is disassembled into subcomplexes of Nups during open mitosis in higher eukaryotic cells. Mitotic disassembly is thought to be triggered by phosphorylation. The best characterized subcomplex is the vertebrate Nup107-160 and the homologous Nup84 subcomplex in Saccharomyces cerevisiae. The Nup107-160 subcomplex has 9 members (Nup160, Nup133, Nup107, Nup96, Nup75, Nup43, Nup37, Seh1 and Sec 13. In the “protocoatomer” hypothesis, this nonameric complex has been proposed to stabilize the sharp bend between the inner and outer nuclear envelope membrane.

Beck, M. and Glavy, J.S. (2014). "Toward understanding the structure of the vertebrate nuclear pore complex", Nucleus, 5 (2), 119-123.

K.H. Bui, A. von Appen, A. L. DiGuilio, L. Sparks, M. Mackmull, T. Bock, W. Hagen, A. Andrés-Pons, J. S. Glavy, and M. Beck. (Dec 5, 2013). "Integrated Structural Analysis of the Human Nuclear Pore Complex Scaffold", Cell, cover. 155 (6), 1233-1243. Article Link .

Li, Z., Zhu, Y., Zhai, Y., Castroagudin, M.R., Bao, Y., White, T.E., Glavy, J.S. (2013). "Werner Complex Deficiency in Cells Disrupts the Nuclear Pore Complex and the Distribution of Lamin B1", Biochimica et Biophysica Acta, 1833 (12), 3338-3345.

Kaur, S., White, T.E., DiGuilio, A.L., Glavy, J.S. (Aug 1, 2010). "The Discovery of a Werner Helicase Interacting Protein (WHIP) Association with the Nuclear Pore Complex", Cell Cycle, 9 (15), 3106-3111.

Blethrow, J.D., Glavy, J.S. Morgan, D.O., and Shokat K.M.. (2008). "Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates. ", PNAS, 105 1442-1447.

Glavy, J. S., Krutchinsky, A., Cristea, I.M., Berke, I.C., Boehmer, T., Blobel, G. and Chait, B.T. (2007). "Cell-Cycle Dependent Phosphorylation of the Nuclear Pore Nup107-160 Subcomplex", PNAS, 104 3811-3816.

Bao, Y., et al.. (Aug 11, 2013). "Detection and Correction of Interference MS1 Quantitation of Peptides Using their Distributions", Download .