Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/119313
Title: REGULATION OF THE NEURONAL-SPECIFIC TRYPTOPHAN HYDROXYLASE-2
Authors: HO SHI YUN
Keywords: Tryptophan hydroxylase, serotonin, heat shock proteins, ubiquitination, protein degradation, protein stability
Issue Date: 29-Sep-2014
Source: HO SHI YUN (2014-09-29). REGULATION OF THE NEURONAL-SPECIFIC TRYPTOPHAN HYDROXYLASE-2. ScholarBank@NUS Repository.
Abstract: DYSREGULATION OF BRAIN SEROTONIN HOMEOSTASIS HAS BEEN IMPLICATED IN MANY NEUROPSYCHIATRIC DISORDERS. TRYPTOPHAN HYDROXYLASE-2 (TPH2) IS THE RATE-LIMITING ENZYME IN BRAIN SEROTONIN SYNTHESIS, AND HAS BEEN SHOWN TO BE UNSTABLE IN VITRO, AS COMPARED TO ITS PERIPHERAL ISOFORM TRYPTOPHAN HYDROXYLASE-1 (TPH1). NEVERTHELESS, MOLECULAR MECHANISMS INVOLVED IN REGULATING TPH2 STABILITY ARE STILL NOT WELL UNDERSTOOD. THIS STUDY HAS IDENTIFIED HEAT SHOCK PROTEIN HSP70 AS A NOVEL TPH-INTERACTING PROTEIN THAT POSITIVELY REGULATES PROTEIN EXPRESSION. HSP70 INTERACTION WITH TPH2 WAS WEAKER, AS COMPARED TO TPH1. TPH2 EXPRESSION WAS ALSO MORE SENSITIVE TO CHANGES IN HSP70 LEVELS, INDICATING THAT THE INSTABILITY OF TPH2 IS PARTLY DUE TO ITS POOR INTERACTION WITH HSP70. THE STUDY ALSO DEMONSTRATED THAT TPH2 UNDERGOES UBIQUITINATION AND PROTEASOMAL DEGRADATION. HOWEVER, LYSINE-LESS TPH2 WAS STILL UBIQUITINATED, INDICATING ALTERNATIVE MECHANISMS IN TPH2 UBIQUITINATION. TAKEN TOGETHER, THIS WORK HAS REVEALED
URI: http://scholarbank.nus.edu.sg/handle/10635/119313
Appears in Collections:Ph.D Theses (Open)

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