My interests include: elucidation of signaling networks relevant to human disease and exploring perturbations in phosphorylation patterns induced by pharmacological agents. Quantitative phosphoproteomic analysis by mass spectrometry is a technique that allows efficient profiling of tens of thousands of phosphorylation sites over time from cells and tissues. Our laboratory employs this platform to map complex signaling networks in T cells to more holistically understand the structure of the T cell signaling pathway.

The reversible phosphorylation of tyrosine, serine, and threonine residues is an important mechanism for modulating biological processes such as cellular signaling, differentiation, and growth. A comprehensive understanding of these dynamic cellular processes at the molecular level requires the simultaneous detection of changes in the sites and levels of phosphorylation across numerous proteins over time and through space within the cell. We employ fully automated, highly selective new methodologies that allow for the simultaneous assignment of the temporal and spatial pattern of phosphorylation sites from exceedingly complex mixtures derived from whole cell lysates. This technological infrastructure is applied to the analysis of complex signaling networks in diverse biological and pharmacological contexts.

Many cellular processes are directly controlled through the reversible phosphorylation of protein tyrosine residues. These regulatory functions are ultimately achieved through the coordinated phosphorylation and dephosphorylation of numerous tyrosine residues across multiple proteins over time. Clearly, benefits arise from individually characterizing specific components of a particular pathway, such as identifying a site of phosphorylation on a given protein, the kinase responsible for the modification, or the phosphatase responsible for its removal, or the identity of proteins that subsequently interact. Ultimately though, a thorough understanding of these signaling pathways at the molecular level requires the thorough, simultaneous evaluation of all phosphorylation and dephosphorylation events—changes in phosphorylation state—over time.

Emerging methodologies in mass spectrometry derive their utility through application to persistent, difficult problems in pharmacology and cellular biology. The ability of the mass spectrometer to assign sites of phosphorylation and ubiquitination in complex mixtures of peptides represents an opportunity to greatly accelerate the elucidation of signaling pathways. Identification of novel signaling pathway members will provide targets for rational development of drugs that selectively inhibit these pathways. Recent successes with the BCR/ABL kinase inhibitor STI571 (Gleevec) in the treatment of chronic myelogenous leukemia and with the HER2 receptor protein tyrosine kinase inhibitor Herceptin in the treatment of advanced breast cancer, illustrate the viability of targeting signaling pathway members to treat disease.

R01 AI083636-01 | (PI: A. Salomon) | 07/01/17 to 6/30/22 | NIH/NIAID
“Phosphoproteomic Analysis of T Cell Activation Pathways”
Role: PI

P30GM110759-01 | (PI: B. Ramratnam) | 5/1/15 to 4/30/20 | NIH/GM
"COBRE Center for Cancer Research Development, Phase 3"
Role: Subcontract PI

P01AI091580 | (PI: A. Weiss) | 7/1/16 to 6/30/21 | NIH/NIAID
"Defining the unique properties of the distinct signaling machinery used by the TCR"
Role: Subcontract PI 

National Institutes of Health Biotechnology Training Grant, 1995-1997
NIH Study Section ZRG1 BST-D(55) National Technology Centers for Networks and Pathways, 2005
NIH Study Section ZRG1 BST-D(51) Continued Development and Maintenance of Software, 2006
Beckman Young Investigator Award, 2006-20010
Session Chair, 96th American Association of Immunologist Annual Meeting "Technological Innovations in Immunology", Seattle, WA, 2009

American Chemistry Society
The American Association of Immunologists

Dr. Salomon’s pedagogical goals at Brown within the classroom have centered upon developing teaching methodology for effective instruction in basic undergraduate biochemistry as well as graduate instruction in interpretation of the primary scientific literature. This methodology was tested in both a lecture course in undergraduate Biochemistry (Bio 28, Spring 2006/7/8/9/10/11/12/14) and a seminar course  (Bio221, Fall 2006/7/8/9) both team taught with Professor Gerwald Jogl from the MCB department.