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Balla, TAMAS

Formal Title:

Senior Investigator


Dr. Balla is heading the Section on Molecular Signal Transduction within the Program for Developmental Neuroscience





35A CONVENT DR Room 2D842, MSC 3752
Bethesda ,MD 20892

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Tamas Balla received his MD degree from Semmelweis University, School of Medicine, Budapest, Hungary in 1979 and earned his Ph.D. from the Hungarian National Academy of Science in 1987. He was appointed as an Assistant Professor in the Department of Physiology at Semmelweis in 1979 and held this position until 1992. He did his postdoctoral training at the NICHD between 1985-87 with Dr. Kevin Catt and returned to the NIH in 1989. He became a tenure-track investigator in 1997 in the Endocrinology and Reproduction Research Branch, leading the Section of Molecular Signal Transduction and received his tenure in 2004. Currently he is a Senior Investigator leading the same Section, which is now part of the Program for Developmental Neuroscience within the NICHD, NIH. In 2009 Dr. Balla received a D.Sc. degree from the Hungarian Academy of Science and was elected into the Hungarian Academy of Science in 2010.

Dr. Balla started his research by studying the receptors and signaling pathways mediating the actions of angiotensin II in the adrenal cortex. As it turned out, these receptors (as many others) utilize the phosphoinositide – phospholipase C -calcium – signaling cascade and the unfolding of this system turned Dr. Balla’s attention to inositol phospholipids. While studying the metabolism of Ins(1,4,5)P3, he and his colleagues discovered a novel pathway that linked Ins(1,4,5)P3 production to highly phosphorylated inositols and that these metabolites showed long-term changes after agonist stimulation. In the mid 90’s he and his colleagues were the first to discover that the signaling pool of phosphoinositides in the plasma membrane is synthesized by type III PI 4-kinases (not by the type II forms as previously believed). He led the efforts to purify and clone these enzymes from bovine adrenal and -brain and study their functions in cellular physiology. The cellular distribution of these enzymes have clearly indicated that their functions are linked to a variety of trafficking events in addition to their roles in receptor signaling. The highly localized inositide changes prompted Dr. Balla to experiment with fluorescent methods to visualize the cellular distribution and dynamics of inositol lipid changes in live cells. His group was one of the firsts to report on live cell imaging of PtdIns(4,5)P2 and PtdIns(3,4,5)P3. Since then his research is primarily concerned with the roles of phosphatidylinositol 4-kinase enzymes in cellular trafficking and signaling. He also continues to focus on improving methods by which to visualize and manipulate phosphoinositides and other lipids in specific cellular compartments in intact living cells.

Dr. Balla has been elected as an outside member of the Hungarian National Academy of Science. He is member of the American Society of Cell Biology, the American Society of Biochemistry and Molecular Biology and the Hungarian Physiological Society. He serves on the Editorial Board of the Journal of Biological Chemistry and Neurochemistry International, and he is an Associate Editor of BMC Cell Biology. He has published over 140 articles and was invited to speak in numerous national and international conferences.

Publications (PubMed):

Two phosphatidylinositol 4-kinases control lysosomal delivery of the Gaucher disease enzyme, ß-glucocerebrosidase.
A highly dynamic ER-derived phosphatidylinositol-synthesizing organelle supplies phosphoinositides to cellular membranes.
Intracellular curvature-generating proteins in cell-to-cell fusion.
A homogeneous and nonisotopic assay for phosphatidylinositol 4-kinases.
Genetic and functional studies of phosphatidyl-inositol 4-kinase type IIIa.
Dependence of STIM1/Orai1-mediated calcium entry on plasma membrane phosphoinositides.
Finding partners for PI3Kgamma: when 84 is better than 101.
Store-operated Ca2+ influx and subplasmalemmal mitochondria.
PI4P and PI(4,5)P2 are essential but independent lipid determinants of membrane identity.
Phosphatidylinositol 4-kinases: hostages harnessed to build panviral replication platforms.
Acute depletion of plasma membrane phosphatidylinositol 4,5-bisphosphate impairs specific steps in endocytosis of the G-protein-coupled receptor.
Recruitment and activation of a lipid kinase by hepatitis C virus NS5A is essential for integrity of the membranous replication compartment.
Activation of STIM1-Orai1 involves an intramolecular switching mechanism.
Demonstration of angiotensin II-induced Ras activation in the trans-Golgi network and endoplasmic reticulum using bioluminescence resonance energy transfer-based biosensors.
Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface.
Viral reorganization of the secretory pathway generates distinct organelles for RNA replication.
Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling.
Putting G protein-coupled receptor-mediated activation of phospholipase C in the limelight.
Dual roles for the Drosophila PI 4-kinase four wheel drive in localizing Rab11 during cytokinesis.
Crucial role of phosphatidylinositol 4-kinase IIIalpha in development of zebrafish pectoral fin is linked to phosphoinositide 3-kinase and FGF signaling.
Green light to illuminate signal transduction events.
Live cell imaging with protein domains capable of recognizing phosphatidylinositol 4,5-bisphosphate; a comparative study.
Phosphoinositide signaling: new tools and insights.
A PH domain in the Arf GTPase-activating protein (GAP) ARAP1 binds phosphatidylinositol 3,4,5-trisphosphate and regulates Arf GAP activity independently of recruitment to the plasma membranes.
Regulation of Ca2+ entry by inositol lipids in mammalian cells by multiple mechanisms.
Visualization of cellular phosphoinositide pools with GFP-fused protein-domains.
STIM and Orai: the long-awaited constituents of store-operated calcium entry.
Enteropathogenic Escherichia coli subverts phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate upon epithelial cell infection.
Live cell imaging of phosphoinositides with expressed inositide binding protein domains.
G protein-coupled receptor-promoted trafficking of Gbeta1gamma2 leads to AKT activation at endosomes via a mechanism mediated by Gbeta1gamma2-Rab11a interaction.
Design of drug-resistant alleles of type-III phosphatidylinositol 4-kinases using mutagenesis and molecular modeling.
Maintenance of hormone-sensitive phosphoinositide pools in the plasma membrane requires phosphatidylinositol 4-kinase IIIalpha.
c-Met must translocate to the nucleus to initiate calcium signals.
A membrane capture assay for lipid kinase activity.
Visualization and manipulation of plasma membrane-endoplasmic reticulum contact sites indicates the presence of additional molecular components within the STIM1-Orai1 Complex.
Dual regulation of TRPV1 by phosphoinositides.
Regulation of connexin43 gap junctional communication by phosphatidylinositol 4,5-bisphosphate.
Visualization and manipulation of phosphoinositide dynamics in live cells using engineered protein domains.
Active Arf6 recruits ARNO/cytohesin GEFs to the PM by binding their PH domains.
Imaging and manipulating phosphoinositides in living cells.
Loss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate.
Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels.
Control of cell polarity and motility by the PtdIns(3,4,5)P3 phosphatase SHIP1.
Nucleolar localization of phosphatidylinositol 4-kinase PI4K230 in various mammalian cells.
Rapidly inducible changes in phosphatidylinositol 4,5-bisphosphate levels influence multiple regulatory functions of the lipid in intact living cells.
Phosphatidylinositol 4-kinase IIIbeta regulates the transport of ceramide between the endoplasmic reticulum and Golgi.
Structural and functional features and significance of the physical linkage between ER and mitochondria.
Phosphatidylinositol 4-kinases: old enzymes with emerging functions.
Live cell imaging of phosphoinositide dynamics with fluorescent protein domains.
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