Suleiman W. Bahouth, Ph.D.

Suleiman W. Bahouth, Ph.D.

Professor
Department of Pharmacology

The University of Tennessee
Health Science Center
Department of Medicine, Division of Cardiovascular Diseases
874 Union Avenue
Memphis, TN 38163
Phone: (901) 448-6009
Fax: (901) 448-7300
Lab: 309 Crowe Research Building
Email: Suleiman W. Bahouth



Education

  • Ph.D. Institution: New York University, Department of Pharmacology
  • Postdoctoral: State University of New York at Stony Brook, Department of Molecular Pharmacology

Links

Pharmacology - Suleiman W. Bahouth

Research Interests

My research program is focused on analyzing the mechanism(s) by which hormones and neurotransmitters regulate transmembranal signalling. The approach involves determining the regions in G protein coupled receptors and GTP binding regulatory proteins (G proteins) that are involved in regulating the sensitivity of the cell to hormones and neurotransmitters.

The sensitivity of the heart to the neurotransmitter norepinephrine or to its circulating counterpart epinephrine, is profoundly influenced by thyroid hormones (T3). In the heart, it appears that the dominant receptor mediating the functions of catecholamines is the beta-adrenergic receptor. T3 upregulate the number of beta-adrenergic receptors in the heart cell and increase their sensitivity to catecholamines. With respect to the receptor, T3 exert their effects by increasing the transcription of the beta-adrenergic receptor gene. The goal of our ongoing studies is to identify the cis-acting DNA sequences in the beta-adrenergic receptor gene and trans-acting nuclear proteins that are involved in the stimulation of beta-adrenergic receptor gene transcription by T3.

The sensitivity of the receptor to catecholamines is modulated by T3 through a complex mechanism operating at a point distal to the receptor. Activation of the beta-adrenergic receptor results in the initiation of a cascade that results in the generation of the intracellular messenger cyclic AMP. The activity of the effector enzyme that catalyzes the conversion of ATP to cyclic AMP is regulated by G proteins. Our studies are focused on identifying the mechanism by which T3 regulate the abundance and coupling of G proteins to the receptor and effector.

Representative Publications

  • Nooh MM, Bahouth SW. Two barcodes encoded by the type-1 PDZ and by phospho-Ser(312) regulate retromer/WASH-mediated sorting of the ß(1)-adrenergic receptor from endosomes to the plasma membrane. Cell Signal. 2017 Jan;29:192-208. doi: 10.1016/j.cellsig.2016.10.014. PubMed PMID: 27816670.
  • Nooh MM, Mancarella S, Bahouth SW. Identification of novel transplantable GPCR recycling motif for drug discovery. Biochem Pharmacol. 2016 Nov 15;120:22-32. doi: 10.1016/j.bcp.2016.09.011. PubMed PMID: 27645110; PubMed Central PMCID: PMC5079812.
  • Li JJ, Ferry RJ Jr, Diao S, Xue B, Bahouth SW, Liao FF. Nedd4 haploinsufficient mice display moderate insulin resistance, enhanced lipolysis, and protection against high-fat diet-induced obesity. Endocrinology. 2015 Apr;156(4):1283-91. doi: 10.1210/en.2014-1909. PubMed PMID: 25607895; PubMed Central PMCID: PMC4399314.
  • Li X, Matta SM, Sullivan RD, Bahouth SW. Carvedilol reverses cardiac insufficiency in AKAP5 knockout mice by normalizing the activities of calcineurin and CaMKII. Cardiovasc Res. 2014 Nov 1;104(2):270-9. doi: 10.1093/cvr/cvu209. PubMed PMID: 25225170; PubMed Central PMCID: PMC4296113.
  • Nooh MM, Chumpia MM, Hamilton TB, Bahouth SW. Sorting of β1-adrenergic receptors is mediated by pathways that are either dependent on or independent of type I PDZ, protein kinase A (PKA), and SAP97. J Biol Chem. 2014 Jan 24;289(4):2277-94. doi: 10.1074/jbc.M113.513481. PubMed PMID: 24324269; PubMed Central PMCID: PMC3900972.
  • Li X, Nooh MM, Bahouth SW. Role of AKAP79/150 protein in β1-adrenergic receptor trafficking and signaling in mammalian cells. J Biol Chem. 2013 Nov 22;288(47):33797-812. doi: 10.1074/jbc.M113.470559. PubMed PMID: 24121510; PubMed Central PMCID: PMC3837123.

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