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2017 | 77 | Suppl.1 |
Tytuł artykułu

The role of s-palmitoylation and s-nitrosylation interplay in the chronic stress disorders

Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
Chronic stress exposure is a key environmental factor for development of neuropsychiatric disorders such as major depression and anxiety disorders. Chronic stress-related emotional and cognitive impairment is associated with alternations in synaptic organization. One of the best described mechanism of synaptic proteins regulation are posttranslational modifications. S-palmitoylation is the covalent lipid reversible modification of cysteine with palmitate which regulates diverse aspects of neuronal protein trafficking and function. The reversible nature of palmitoylation allows proteins to associate with membranes, what regulate their sorting, localization and functions. Intracellular protein S-palmitoylation is controlled by family of protein acyl-transferases and palmitoyl-thioesterases. Recent study shows alternative mechanism of S-palmitoylation regulation by S-nitrosylation. S-nitrosylation is the covalent modification of cysteine by a nitric oxide (NO). The main aim is to understand the functional consequences of alerted protein S-palmitoylation and S-nitrosylation interplay induced by chronic restraint stress. Using mass spectrometry based approaches we profiled endogenous S-palmitoylation and S-nitrosylation. We identified massive changes at the level of proteins and exact sites of modifications in the mouse model of chronic stress. In the physiological conditions we observed excellent competitive effect, over 50% of cysteines were identified only in the one form S-nitrosylated or S-palmitoylated. After chronic stress, we demonstrated that almost all identified proteins were simultaneously modified by palmitate and NO. Summarizing, our results suggest that altered mechanism of interplay between S-palmitoylation and S-nitrosylation of synaptic proteins might be one of the main events associated with chronic stress disorder, leading to destabilization in synaptic networks. FINANCIAL SUPPORT: Financial Support: NCN OPUS 2015/17/B/NZ3/00557.
Słowa kluczowe
Wydawca
-
Rocznik
Tom
77
Numer
Opis fizyczny
p.32
Twórcy
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warsaw, Poland
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warsaw, Poland
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warsaw, Poland
autor
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warsaw, Poland
autor
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warsaw, Poland
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warsaw, Poland
Bibliografia
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-9154628f-9493-4642-8b89-ad9e53f18156
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