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Faculty Detail     Name BAKHROM K BERDIEV   Campus Address MCLM 725 Zip 0005 Phone 205-934-2389 E-mail berdiev@uab.edu Other websites

Faculty Appointment(s) Appointment Type Department Division Rank Primary  Cell, Developmntl, & Integrative Biology  Cell, Developmntl, & Integrative Biology Assistant Professor Secondary  Physiology & Biophysics   Physiology & Biophysics Assistant Professor Center  Cystic Fibrosis Research Center  Cystic Fibrosis Research Center Assistant Professor

Graduate Biomedical Sciences Affiliations Cell, Molecular, & Developmental Biology  Neuroscience  Pathobiology and Molecular Medicine

Biographical Sketch  Dr. Bakhrom K. Berdiev, Assistant Professor of Cell Biology, received his M.D. in 1988 from the Pediatric Institute in Tashkent, Soviet Union, and Ph.D. in 1996 from Tashkent Institute of Physiology and Biophysics, Uzbekistan. He came to UAB Department of Physiology and Biophysics in 1997 as a postdoctoral fellow and joined the Physiology and Biophysics faculty in 2003. In 2007 Dr. Berdiev joined the Department of Cell Biology.

Research/Clinical Interest Title The CFTR Chloride Channel control of Epithelial Sodium Channel under physiological and pathological conditions. Description Our interests revolve around two membrane proteins: the cystic fibrosis transmembrane conductance regulator (CFTR) and the epithelial Na channel (ENaC). CFTR functions not only as a chloride channel, but also has a remarkable ability to affect the function of other ion transporting pathways. One of these proteins is ENaC. ENaC transports sodium ions across epithelia and is likely best known for being involved in hypertension. Their relationship, along with mutations in CFTR, shapes the pathophysiology of cystic fibrosis: a mutated CFTR is unable to restrict sodium flow through ENaC leading to increased sodium absorption across airway epithelia, which in turn causes an increase in mucus viscosity and a reduction in mucociliary clearance, ultimately leading to bacterial colonization To study CFTR, ENaC, and their relationship we use an integrative approach which includes the combination of electrophysiology, molecular biology, biochemistry with special emphasis on variations of fluorescence microscopy based on Fluorescence Resonance Energy Transfer (FRET). FRET exploits the exquisite sensitivity of fluorescence measurements to detect molecular complexes with near angstrom resolution. The FRET principle is based on the following concept: if two fluorescent proteins, a donor and acceptor, are sufficiently close (≤10 nm), radiation-less (i.e. not mediated by photons) transfer of energy from donor to acceptor can be observed after excitation of the donor. Both the rate and the efficiency of energy transfer are directly related to the distance between the donor and acceptor. If the fluorophores are more than 10 nm apart, no FRET will be detected. Using this technique, one can estimate the distance between two molecules, and establish whether proteins that appear to be co-localized by conventional optical microscopy actually interact with each other. Recently, we have found the evidence for a direct physical association of CFTR and ENaC. We have used FRET to estimate the proximity of CFTR and ENaC - an essential variable for possible physical interaction to occur. We complemented our FRET studies with classical biochemical approaches – coimmunoprecipitation and colocalization. Our results place CFTR and ENaC within reach of each other, suggestive of a direct interaction between these two proteins.

Selected Publications  Publication PUBMEDID Berdiev BK, Cormet-Boyaka E, Tousson A, Qadri YJ, Oosterveld-Hut HM, Hong JS, Gonzales PA, Fuller CM, Sorscher EJ, Lukacs GL, Benos DJ.Molecular proximity of CFTR and ENaC assessed by fluorescence resonance energy transfer.J Biol Chem. 2007 Oct 3; [Epub ahead of print]  17913705  Berdiev BK, Benos DJ.Epithelial sodium channel in planar lipid bilayers.Methods Mol Biol. 2006;337:89-99.  16929941  Berdiev BK, Jovov B, Tucker WC, Naren AP, Fuller CM, Chapman ER, Benos DJ.ENaC subunit-subunit interactions and inhibition by syntaxin 1A.Am J Physiol Renal Physiol. 2004 Jun;286(6):F1100-6. Epub 2004 Mar 2.  14996668  Berdiev BK, Xia J, McLean LA, Markert JM, Gillespie GY, Mapstone TB, Naren AP, Jovov B, Bubien JK, Ji HL, Fuller CM, Kirk KL, Benos DJ.Acid-sensing ion channels in malignant gliomas.J Biol Chem. 2003 Apr 25;278(17):15023-34. Epub 2003 Feb 12.  12584187  Berdiev BK, Xia J, Jovov B, Markert JM, Mapstone TB, Gillespie GY, Fuller CM, Bubien JK, Benos DJ.Protein kinase C isoform antagonism controls BNaC2 (ASIC1) function.J Biol Chem. 2002 Nov 29;277(48):45734-40. Epub 2002 Sep 19.  12244121  Berdiev, B.K., T.B. Mapstone, J.M. Markert, G.Y. Gillespie, J. Lockhart, C.M. Fuller, and D.J. Benos. pH alterations "reset" Ca2+ sensitivity of brain Na+ channel 2, a degenerin/epithelial Na+ ion channel, in planar lipid bilayers. J. Biol. Chem. 276:38755‑38761, 2001.  11514582  Berdiev, B.K., T.B. Mapstone, J.M. Markert, G.Y. Gillespie, J. Lockhart, C.M. Fuller, and D.J. Benos. pH alterations "reset" Ca2+ sensitivity of brain Na+ channel 2, a degenerin/epithelial Na+ ion channel, in planar lipid bilayers. J. Biol. Chem. 276:38755‑38761, 2001.  11514582  Berdiev BK, Latorre R, Benos DJ, Ismailov II.Actin modifies Ca2+ block of epithelial Na+ channels in planar lipid bilayers.Biophys J. 2001 May;80(5):2176-86.  11325720  Berdiev BK, Shlyonsky VG, Karlson KH, Stanton BA, Ismailov II.Gating of amiloride-sensitive Na(+) channels: subunit-subunit interactions and inhibition by the cystic fibrosis transmembrane conductance regulator.Biophys J. 2000 Apr;78(4):1881-94.  10733968

Keywords CFTR, ENaC, ASICs, Bilayers, FRET

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