Proceedings of the National Academy of Sciences of the United States of America

About the PNAS Member Editor
Name Weiss, Arthur
Location University of California, San Francisco
Primary Field Immunology and Inflammation
Secondary Field Medical Genetics, Hematology and Oncology
 Election Citation
Weiss is an immunologist who has made major contributions to our understanding of the signaling mechanisms that regulate T lymphocyte development and response. He has identified a novel cytoplasmic tyrosine kinase, defined its role in a congenital immunodeficiency disease, and delineated the mechanisms by which both cytoplasmic tyrosine kinases and transmembrane tyrosine phosphatases control T cell signaling.
 Research Interests
I'm interested in understanding the signaling mechanisms involved in regulating T lymphocyte development and responses. We've focused mainly on signal transduction by the T cell receptor (TCR) for antigen. The TCR is an oligomeric structure, consisting of the products of 6 genes. To understand the TCR structural complexity, we used chimeric receptors and found that the receptor's invariant chains use common sequence motifs to couple the antigen recognition subunit of the TCR to cytoplasmic Src and Syk/ZAP-70 protein tyrosine kinase families. These two families of kinases interact with the receptor in a sequential and highly coordinated manner, a paradigm used by other immune cell antigen receptors. We're interested in how the process of receptor signaling via cytoplasmic tyrosine kinases is initiated, regulated, and terminated. We've used somatic cell genetics to define critical signaling components downstream of the TCR, including two adaptors that appear to be involved in assembling a scaffold for a signaling complex. We'd like to understand the assembly of the signaling complex and how this complex is regulated. Since tyrosine phosphorylation plays a key role in TCR signals, we've become interested in the function of transmembrane tyrosine phosphatases such as CD45. CD45 regulates the Src family kinases within the TCR signaling pathway. Surprisingly, dimerization of CD45 inhibits its catalytic function via a wedge-like structure in the CD45 juxtamembrane domain. We'd like to understand how dimerization is regulated and its importance in the immune system.

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