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Titus Boggon, PhD

Associate Professor of Pharmacology and of Molecular Biophysics and Biochemistry

Contact Information

Titus Boggon, PhD

Lab Location

Office Location

Mailing Address

  • Pharmacology

    PO Box 208066, 333 Cedar Street

    New Haven, CT 06520-8066

    United States

Boggon Lab

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 cerebral vascular disease. We maintain a focus on the protein kinases involved in these areas.

Coauthors

Research Interests

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

Research Images

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

Selected Publications

  • The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase.Stiegler AL, Boggon TJ. The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase. Structure (London, England : 1993) 2018, 26: 1451-1461.e4. PMID: 30174148, PMCID: PMC6249675, DOI: 10.1016/j.str.2018.07.015.
  • p190RhoGAP proteins contain pseudoGTPase domains.Stiegler AL, Boggon TJ. p190RhoGAP proteins contain pseudoGTPase domains. Nature Communications 2017, 8: 506. PMID: 28894085, PMCID: PMC5593906, DOI: 10.1038/s41467-017-00483-x.
  • CDC42 binds PAK4 via an extended GTPase-effector interface.Ha BH, Boggon TJ. CDC42 binds PAK4 via an extended GTPase-effector interface. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 531-536. PMID: 29295922, PMCID: PMC5776996, DOI: 10.1073/pnas.1717437115.
  • Structural Basis for Noncanonical Substrate Recognition of Cofilin/ADF Proteins by LIM Kinases.Hamill S, Lou HJ, Turk BE, Boggon TJ. Structural Basis for Noncanonical Substrate Recognition of Cofilin/ADF Proteins by LIM Kinases. Molecular Cell 2016, 62: 397-408. PMID: 27153537, PMCID: PMC4860616, DOI: 10.1016/j.molcel.2016.04.001.
  • Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex.Fisher OS, Deng H, Liu D, Zhang Y, Wei R, Deng Y, Zhang F, Louvi A, Turk BE, Boggon TJ, Su B. Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex. Nature Communications 2015, 6: 7937. PMID: 26235885, PMCID: PMC4526114, DOI: 10.1038/ncomms8937.
  • CCM2-CCM3 interaction stabilizes their protein expression and permits endothelial network formation.Draheim KM, Li X, Zhang R, Fisher OS, Villari G, Boggon TJ, Calderwood DA. CCM2-CCM3 interaction stabilizes their protein expression and permits endothelial network formation. The Journal Of Cell Biology 2015, 208: 987-1001. PMID: 25825518, PMCID: PMC4384732, DOI: 10.1083/jcb.201407129.
  • Identification of a major determinant for serine-threonine kinase phosphoacceptor specificity.Chen C, Ha BH, Thévenin AF, Lou HJ, Zhang R, Yip KY, Peterson JR, Gerstein M, Kim PM, Filippakopoulos P, Knapp S, Boggon TJ, Turk BE. Identification of a major determinant for serine-threonine kinase phosphoacceptor specificity. Molecular Cell 2014, 53: 140-7. PMID: 24374310, PMCID: PMC3898841, DOI: 10.1016/j.molcel.2013.11.013.
  • Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation.Liu W, Draheim KM, Zhang R, Calderwood DA, Boggon TJ. Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation. Molecular Cell 2013, 49: 719-29. PMID: 23317506, PMCID: PMC3684052, DOI: 10.1016/j.molcel.2012.12.005.
  • Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate.Ha BH, Davis MJ, Chen C, Lou HJ, Gao J, Zhang R, Krauthammer M, Halaban R, Schlessinger J, Turk BE, Boggon TJ. Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 16107-12. PMID: 22988085, PMCID: PMC3479536, DOI: 10.1073/pnas.1214447109.
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