Harry T. Haigler
Professor Physiology/Biophysics and Assoc. Dean, Medical Education
School of Medicine
School of Medicine
PH.D., Vanderbilt University, 1977
University of California, Irvine
C337 MED SCI I
Mail Code: 4560
Irvine, CA 92697
C337 MED SCI I
Mail Code: 4560
Irvine, CA 92697
Research Abstract
Growth factor signal transduction; annexin calcium-binding proteins
Dr. Haigler's long-term goal is to understand the molecular and cellular mechanisms by which the hormone epidermal growth factor (EGF) controls growth and differentiation of eukaryotic cells. The EGF mitogenic pathway is activated by phosphorylation of certain regulatory proteins. Annexin I was found to be a high-affinity substrate for the EGF-stimulated kinase and to undergo reversible calcium-dependent binding to phospholipids on the cytosolic face of the plasma membrane. Recent research is directed toward determining the biological function of annexin A1, how this function is modulated by phosphorylation, and the role it plays in transduction of the EGF-induced mitogenic signal.
Dr. Haigler also is using the interaction of annexin B12 with phospholipid bilayers as a model system to study the molecular mechanism of annexin:membrane interaction.
Dr. Haigler's long-term goal is to understand the molecular and cellular mechanisms by which the hormone epidermal growth factor (EGF) controls growth and differentiation of eukaryotic cells. The EGF mitogenic pathway is activated by phosphorylation of certain regulatory proteins. Annexin I was found to be a high-affinity substrate for the EGF-stimulated kinase and to undergo reversible calcium-dependent binding to phospholipids on the cytosolic face of the plasma membrane. Recent research is directed toward determining the biological function of annexin A1, how this function is modulated by phosphorylation, and the role it plays in transduction of the EGF-induced mitogenic signal.
Dr. Haigler also is using the interaction of annexin B12 with phospholipid bilayers as a model system to study the molecular mechanism of annexin:membrane interaction.
Publications
Torsten Fischer, T., Lu, L., Haigler, H. T., Langen, R. Annexin B12 is a Sensor of Membrane Curvature and Undergoes Major Curvature-dependent Structural Changes (2007) J. Biol. Chem. 282: 9996-10004
Patel, D. R., Isas, J. M., Ladokhin, A. S., Jao, C. C., Kim, Y. E., Kirsch, T., Langen, R., Haigler, H. T. The Conserved Core Domains of Annexins A1, A2, A5 and B12 Can Be Divided into Two Groups with Different Ca2+-Dependent Membrane Binding Properties. (2005) Biochemistry 44:2833-2844.
Langen, R., Isas, J. M., Hubbell, W. L. and Haigler, H. T. (1998) A transmembrane form of annexin XII detected by site-directed spin labeling. Proc. Natl. Acad. Sci. 95:14060-14065.
Isas, J. M., Langen, R., Hubbell, W. L, Haigler, H. T. Structure and Dynamics of a Helical Hairpin that Mediates Calcium-dependent Membrane Binding of Annexin B12. (2004) J. Biol. Chem. 279: 32492-32498.
Luecke, H., B.T. Chang, W.S. Mailliard,., D.D. Schlaepfer and H.T. Haigler. l995. Crystal structure of the annexin XII hexamer and implications for bilayer insertion. Nature 378: 512-515. (the broad implications of this study are discussed in the "News and Views" article on p. 446-447 of the same issue)
Graduate Programs
Cancer Biology
Structural Biology and Molecular Biophysics
Link to this profile
https://faculty.uci.edu/profile/?facultyId=2301
https://faculty.uci.edu/profile/?facultyId=2301
Last updated
02/08/2010
02/08/2010