Research Interests

Writing, reading and erasing the embryonic epigenetic code

Research Area

The Shechter Lab is in the Depart­ment of Bio­chem­istry at the Albert Ein­stein Col­lege of Med­i­cine in the Bronx, NY. Our research focuses on a “bottom-up” bio­chem­i­cal under­stand­ing of the nature of embry­onic chro­matin, in par­tic­u­lar the role of the his­tone pro­teins and his­tone post-translational modifications. We use eggs and oocytes of the African clawed frog, Xeno­pus lae­vis, as the major model sys­tem in our lab­o­ra­tory (in addi­tion to recom­bi­nant pro­teins and cul­tured cells). The eggs and cell-free extracts of the eggs of the frog Xeno­pus lae­vis were the first sys­tem used for somatic-cell nuclear trans­fer cloning exper­i­ments almost a half-century ago and have been exten­sively used for char­ac­ter­i­za­tion of devel­op­ment, cell-cycle pro­gres­sion, and DNA repli­ca­tion. The cell-free extracts reca­pit­u­late most bio­log­i­cal phe­nom­ena in a bio­chem­i­cally dis­sectible form, in which com­po­nents can be added and removed and small-molecules can be applied. Xeno­pus are the lab­o­ra­tory animal

Current Members

Shechter, David (Principal Investigator/Director)

Additional Information

Our goal to understand how the eukaryotic genome is packaged with histones into chromatin and how chromatin is propagated, expressed, and those transcripts spliced into mature gene transcripts. To improve our basic understanding of biology, human diseases like cancer and ALS, and also to develop new therapeutic approaches, we aim to understand how these processes work and how they are regulated by the cell. Our studies are critically important for understanding diseases such as lung cancer and leukemia, and have wide-ranging implications for human development and neuroscience. Our current primary research interests are: -Protein Arginine Methyltransferases (PRMTs1-9), their protein substrates, and the "readers" of methylarginine -Small molecule methyltransferases in cancer (GNMT, glycine N-methyltransferase regulation of SAM abundance in metastatic prostate cancer) -Histone chaperone proteins (NPM1, NPM2, and NAP1) and structural and molecular mechanisms of their intrinsically disordered regions -Chaperone post-translational glutamylation and deglutamylation by the TTLL and CCP protein families

Contact

Institution: Albert Einstein College of Medicine

Address:
Department of Biochemistry
ack and Pearl Resnick Campus
Bronx, New York
USA

Web Page: http://www.shechterlab.org