Titus Boggon, PhD

Associate Professor of Pharmacology and of Molecular Biophysics and Biochemistry

Research Departments & Organizations

Molecular Biophysics and Biochemistry

Structural Biology

Vascular Biology and Therapeutics Program

WHRY Pilot Project Program Investigators

Yale Cancer Center: Signal Transduction

Office of Cooperative Research

Research Interests

Biochemistry; Crystallography; Hemangioma, Cavernous, Central Nervous System; Molecular Biology; Protein Kinases; Signal Transduction; Substrate Specificity

Research Summary

Cellular signaling cascades that control cytoskeletal remodeling, adhesion, and migration, are critical to life. The Boggon lab uses structural biology and associated techniques to define the molecular level details that control these pathways. Our primary areas of interest are Rho GTPase and integrin signaling pathways, and the molecular basis for acquisition of a devastating disease, cerebral cavernous malformations (CCM). We maintain a focus on the protein kinases involved in these areas.

Selected Publications

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Contact Info

Titus Boggon, PhD
Lab Location
Sterling Hall of Medicine, B-Wing
333 Cedar Street, Ste Suite 302

New Haven, CT 06510
Office Location
Sterling Hall of Medicine, B-Wing
333 Cedar Street, Ste SHM B316A

New Haven, CT 06510
Mailing Address
PharmacologyPO Box 208066
333 Cedar Street

New Haven, CT 06520-8066

Boggon Lab

Rho GTPase signaling cascades

Signaling from Rho family small GTPases represent key cascades that regulate the actin cytoskeleton. We are interested in understanding the regulation mechanisms for these cascades, and how specificity in these pathways is achieved. We wish to discover molecular level details that more fully describe Rho family kinase signaling cascades. See our publications in: Nature Communications, 2017 Molecular Cell, 2014, 2016 Nature Genetics, 2012 PNAS, 2012, 2013, 2018 Structure, 2018 Journal of Cell Science, 2016 BBA, 2018 PLOS ONE, 2013 Review: Journal of Biological Chemistry, 2015

Pseudoenzymes

The spatial organization of amino acids within a conserved fold defines enzyme classes, however, all enzyme classes contain ‘pseudoenzymes’ in which the conserved catalytic residues are degenerate. The ‘pseudo’ members of nucleotide binding enzyme families can be classified with (i) lost nucleotide binding and consequent lost catalytic competence, (ii) retained nucleotide binding but lost catalytic competence, and (iii) retained catalytic activity. These pseudoenzymes are emerging as a significant mediators and regulators of signal transduction. We are probing the structure and function of a number of these proteins. See our publications in: Nature Communications, 2017 Structure, 2018 Journal of Biological Chemistry, 2018 Molecular Cell, 2013

Cerebral Cavernous Malformations (CCM)

Normal regulation of signal transduction by the CCM proteins is lost in CCM disease. This is associated with formation of mulberry-shaped blood vessels in the brain or spine, which can have major complications. Some of the major changes in signaling are alterations in Rho cascades. We have determined the first crystal structures that describe each of the three CCM proteins and are using structure-directed functional approach to discover their roles and importance in signal transduction. See our publications in: Developmental Cell, 2013 FEBS Letters, 2013 Molecular Cell, 2013 Nature Communications, 2015 Journal of Biological Chemistry, 2010, 2011, 2012, 2014, 2015 Journal of Cell Biology, 2015 Journal of Structural Biology, 2015 Science Signaling, 2010 Reviews: Cellular and Molecular Life Sciences, 2014 Journal of Cell Science, 2014 Oncotarget, 2015