Titus Boggon, PhD

Associate Professor of Pharmacology and of Molecular Biophysics and Biochemistry

Departments & Organizations

Pharmacology: Primary Faculty

Molecular Biophysics and Biochemistry

Structural Biology

Vascular Biology and Therapeutics Program

WHRY Pilot Project Program Investigators

Yale Cancer Center: Signal Transduction

Yale Combined Program in the Biological and Biomedical Sciences (BBS): Biochemistry, Quantitative Biology, Biophysics and Structural Biology (BQBS) | Molecular Medicine, Pharmacology, and Physiology

Office of Cooperative Research


Dr. Boggon is a structural biologist interested in the molecular basis of cytosolic signal transduction cascades. He completed his Ph.D. at the University of Manchester, U.K., and postdoctoral studies at Mount Sinai School of Medicine, Columbia University and the Dana-Farber Cancer Institute (at Harvard Medical School). His lab is interested in understanding how RhoGTPase signal transduction pathways are regulated at the molecular level, and the molecular basis for acquisition of a  cerebrovascular disorder,  Cerebral Cavernous Malformations (CCM).

Education & Training

PhD University of Manchester, UK (1998)
BS University of Manchester, UK (1995)
Research Fellow Harvard Medical School and Dana-Farber Cancer Institute
Postdoctoral Scientist Columbia University
Postdoctoral Fellow Mount Sinai School of Medicine

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

New Haven, CT 06510
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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


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