The COP9 signalosome, or the CSN, is a multi-protein complex is known to be part of the regulated (ubiquitin) protein degradation pathway. One biochemical function is its isopeptidase activity for cleavage of Nedd-like proteins from protein targets (deneddylase). We study this protein assembly, comprising 8 subunits (CSN1-8) in collaboration with the lab of Danny Chamovitz (TAU), with the goal of gaining greater insight into its varied functions using a structural and biophysical angle.
RGK G-proteins (Gem, Rad, Rem, Rem2)
Small G-proteins, which bind guanosine nucleotides, serve as molecular switches in different contexts. The hundreds of proteins in this class, also called the Ras superfamily, have two states: on (GTP-bound) or off (GDP-bound). Most of these proteins have intrinsic catalytic activity, enabling them to hydrolyse GTP, forming GDP. We have been investigating the structure-function relationships of the RGK family that has unusual biochemical properties and regulate calcium channels and Rho kinase.