Posts classified under: Physiology

H. Ronald Kaback, M.D.


H. Ronald Kaback has been a member of the faculty at UCLA since he joined the Depts. of Physiology and Microbiology, Immunology & Molecular Genetics, as well as the Molecular Biology Institute, in 1989 as a full professor. Dr. Kaback earned his B.S. at Haverford College and his M.D. at The Albert Einstein College of Medicine, where he also did an internship in Pediatrics. After a year as a graduate student, he became a Commissioned Officer in the USPHS at the NIH and subsequently became at Staff Associate. He then moved to the Roche Institute of Molecular Biology in Nutley, NJ where he later became Head of Biochemistry before coming to UCLA. He is a member of the National Academy of Science and is the recipient of many awards for his work.


A selected list of publications:

Zhou, Y. Guan, L. Kaback, H. R.   Opening and closing of the periplasmic gate in lactose permease, Proc Natl Acad Sci U S A, 2008; in press.
Nie, Y. Ermolova, N. Kaback, H. R.   Site-directed Alkylation of LacY: Effect of the Proton Electrochemical Gradient J Mol Biol, 2007; 374(2): 356-64.
Smirnova, I. Kasho, V. Choe, J. Y. Altenbach, C. Hubbell, W. L. Kaback, H. R.   Sugar binding induces an outward facing conformation of LacY Proc Natl Acad Sci U S A, 2007; 104: 16504-16509.
Guan, L. Mirza, O. Verner, G. Iwata, S. Kaback, H. R.   Structural determination of wild-type lactose permease Proc Natl Acad Sci U S A, 2007; 104(39): 15294-8.
Majumdar, D. S. Smirnova, I. Kasho, V. Nir, E. Kong, X. Weiss, S. Kaback, H. R.   Single-molecule FRET reveals sugar-induced conformational dynamics in LacY Proc Natl Acad Sci U S A, 2007; 104(31): 12640-12645.
Guan, L. Kaback, H. R.   Site-directed alkylation of cysteine to test solvent accessibility of membrane proteins Nat Protoc, 2007; 2(8): 2012-7.
Shimohata, N. Nagamori, S. Akiyama, Y. Kaback, H. R. Ito, K.   SecY alterations that impair membrane protein folding and generate a membrane stress J Cell Biol, 2007; 176(3): 307-17.
Smirnova, I. N. Kasho, V. N. Kaback, H. R.   Direct Sugar Binding to LacY Measured by Resonance Energy Transfer Biochemistry, 2006; 45(51): 15279-87.
Kaback, H. R. Dunten, R. Frillingos, S. Venkatesan, P. Kwaw, I. Zhang, W. Ermolova, N.   Site-directed alkylation and the alternating access model for LacY Proc Natl Acad Sci U S A, 2006; .
Guan, L. Kaback, H. R.   Lessons from Lactose Permease Annu Rev Biophys Biomol Struct, 2006; 35: 67-91.
Nie, Y. Smirnova, I. Kasho, V. Kaback, H. R.   Energetics of Ligand-induced Conformational Flexibility in the Lactose Permease of Escherichia coli J Biol Chem, 2006; 281(47): 35779-84.
Vadyvaloo, V. Smirnova, I. N. Kasho, V. N. Kaback, H. Ronald   Conservation of residues involved in sugar/H(+) symport by the sucrose permease of Escherichia coli relative to lactose permease J Mol Biol, 2006; 358(4): 1051-9.
Kasho, V. N. Smirnova, I. N. Kaback, H. R.   Sequence alignment and homology threading reveals prokaryotic and eukaryotic proteins similar to lactose permease J Mol Biol, 2006; 358(4): 1060-70.
Ermolova, N. Madhvani, R. V. Kaback, H. R.   Site-directed alkylation of cysteine replacements in the lactose permease of Escherichia coli: helices I, III, VI, and XI Biochemistry, 2006; 45(13): 4182-9.
Mirza, O. 2006)200251183Guan, L. Verner, G. Iwata, S. Kaback, H. R.   Structural evidence for induced fit and a mechanism for sugar/H(+) symport in LacY Embo J, 2006; 25: 1177-1183.
Guan, L. Smirnova, I. N. Verner, G. Nagamoni, S. Kaback, H. R.   Manipulating phospholipids for crystallization of a membrane transport protein Proc Natl Acad Sci U S A, 2006; 103(6): 1723-6.
Kaback, H. R.   Structure and mechanism of the lactose permease C R Biol, 2005; 328(6): 557-67.
Kaback, H. R   The Passion of the Permease, Biophysical and Structural Aspects of Bioenergetics, 2005; 359-373.
Ermolova, N. V. Smirnova, I. N. Kasho, V. N. Kaback, H. R.   Interhelical packing modulates conformational flexibility in the lactose permease of Escherichia coli Biochemistry, 2005; 44(21): 7669-77.
van Bloois, E. Nagamori, S. Koningstein, G. Ullers, R. S. Preuss, M. Oudega, B. Harms, N. Kaback, H. R. Herrmann, J. M. Luirink, J.   The Sec-independent function of Escherichia coli YidC is evolutionary-conserved and essential J Biol Chem, 2005; 280(13): 12996-3003.
Weinglass, A. B. Soskine, M. Vazquez-Ibar, J. L. Whitelegge, J. P. Faull, K. F. Kaback, H. R. Schuldiner, S.   Exploring the role of a unique carboxyl residue in EmrE by mass spectrometry J Biol Chem, 2005; 280(9): 7487-92.
Sun, J. Savva, C. G. Deaton, J. Kaback, H. R. Svrakic, M. Young, R. Holzenburg, A.   Asymmetric binding of membrane proteins to GroEL Arch Biochem Biophys, 2005; 434(2): 352-7.

Baljit Khakh, Ph.D.


Baljit S. Khakh received a Ph.D. degree from the University of Cambridge in 1995. During his graduate studies, he also spent some time at the Geneva Biomedical Research Institute. Dr. Khakh completed a postdoctoral fellowship in the laboratory of Dr. Graeme Henderson at the University of Bristol, followed by a fellowship at the California Institute of Technology, working in the laboratories of Drs. Henry A. Lester and Norman Davidson as a Wellcome Trust International Prize Traveling Research Fellow, and Senior Research Fellow in the Division of Biology. In 2001, Dr. Khakh returned to Cambridge in the Division of Neurobiology at the MRC Laboratory of Molecular Biology. Dr. Khakh joined UCLA in April 2006.

Istvan Mody, Ph.D.


Synaptic Signaling in Health and Disease Our research focuses on 1) the physiology, pharmacology, and pathology of synaptic transmission in the mammalian brain, and 2) the regulation of intracellular calcium homeostasis. The two themes ultimately converge in our quest for understanding how long-term alterations in the excitability of nerve cells and circuits are responsible for offsetting the frail balance between excitation and inhibition. Tipping this balance, either acutely of chronically, results in the nervous system showing signs of abnormal activity leading to specific brain disorders. We study synaptic transmission and the activation of extrasynaptic receptors in the healthy and the diseased brain. We presently carry out research in animal models of epilepsy, Huntington’s disease, stress, alcoholism, PMS/PMDD, postpartum depression, while also recording from human brain tissue surgically removed for the treatment of epilepsies. By studying the fundamental mechanisms responsible for the altered synapses and circuits our studies will lead to novel therapies for a number of devastating neurological and psychiatric disorders. The experimental approaches we use include patch-clamp recordings (whole-cell, single channel and perforated patch) in brain slices, in acutely isolated animal and human neurons, or in cultured neurons/slices; chronic recordings in vivo to monitor long-term changes in the excitability of circuits; infrared and fluorescent video microscopy and simultaneous recordings in live brain tissue; various neuroanatomical and immunohistochemical techniques; measurement of intraneuronal calcium and the binding kinetics of calcium to various calcium-binding proteins; molecular biological approaches aimed at reducing or altering specific brain proteins as in genetic knockouts/knockins and various methods aimed at altering cellular protein levels.