Marco Ceruso

 Many of the biological processes which necessitate that a cell "be" aware of its environment, involve transmission of signals across the plasma membrane. The transmission of these signals is often mediated by protein receptors located within the plasma membrane. These membrane receptors connect the inside of the cell to the extracellular "world". There exist many classes of such membrane receptors that have evolved to recognize a variety of signaling entities such as ions, hormones, or even photons, and the messages carried by such entities regulate processes ranging from gene expression, apoptosis, cell proliferation to higher-order processes such as vision, memory, and learning.

 

 Signaling entities (ligands) generally interact with their cognate receptor on or near the extracellular side of the plasma membrane. This recognition event is often sufficient to elicit the biological function (.i.e. the activation) of the receptor. Activated receptors in turn activate downstream protein substrates located in the intracellular side of the plasma membrane, thereby completing the transmission of the initial signal across the membrane.

 

 Our lab is interested in elucidating how some of these receptors, namely Epidermal Growth Factor Receptors and Ionotropic Glutamate Receptors, accomplish the transmission of the extracellular signal: i.e. what conformational changes does a receptor undergo following the recognition of the ligand, how do these conformational changes support the transmission of the signal across the membrane, and how do the conformational changes and putative downstream interactions of the receptor affect its interaction with the ligand.

 

Cohen L.S., Arshava B., Estephan R., Jacqueline Englander, Kim H., Hauser M, Zerbe O, Ceruso M, Becker J.M., and Naider F. “Expression and biophysical analysis of two double transmembrane domain-containing fragments from a yeast G protein-coupled receptor”. Biopolymers. (2008) 90, 117-30.

 

Basdevant N., Weinstein H., Ceruso M. “Thermodynamic basis for promiscuity and selectivity in protein-protein interactions: PDZ domains, a case study”. J. Am. Chem. Soc. (2006) 128, 12766-77.

 

Ceruso M., Periole X., Weinstein H. Molecular dynamics simulations of transducin: Interdomain and front to back communication in activation and nucleotide exchange. J. Mol. Biol. (2004) 338, 469-481.

 

Periole X., Ceruso M., Mehler E. “Acid-base equilibria in rhodopsin: dependence of the protonation state of Glu134 on its environment”. Biochemistry (2004) 43, 6858-6864.

 

Ceruso M., Grottesi A., Di Nola A. “Dynamic effects of mutations within two loops of cytochrome c551 from Pseudomonas aeruginosa”. Proteins (2003) 50, 222-229.

 

Ceruso M., Weinstein H. “Structural mimicry of proline kinks: tertiary packing interactions support local structural distortions”. J. Mol. Biol. (2002) 318, 1237-1249.

 

Ceruso M., Amadei A., Di Nola A. “Mechanics and dynamics of B1 Domain of protein G: role of packing and surface hydrophobic residues”. Protein Sci. (1999) 8, 147-160.