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1.
Trends Neurosci Educ ; 30: 100200, 2023 03.
Article in English | MEDLINE | ID: mdl-36925267

ABSTRACT

BACKGROUND: This study aimed at investigating the interaction between genetic and environmental factors in predicting executive function in children aged four to six years. METHODS: Response inhibition as index of EF was assessed in 197 children using a go/nogo task. A cumulative dopamine (DA) genetic score was calculated, indexing predisposition of low DA activity. Dimensions of parenting behavior and parental education were assessed. RESULTS: Parental education was positively related to accuracy in nogo trials. An interaction between the cumulative genetic score and the parenting dimension Responsiveness predicted go RT indicating that children with a high cumulative genetic score and high parental responsiveness exhibited a careful response mode. CONCLUSION: The development of EF in kindergarten children is related to parental education as well as to an interaction between the molecular-genetics of the DA system and parenting behavior.


Subject(s)
Dopamine , Executive Function , Humans , Child , Executive Function/physiology , Dopamine/physiology , Parenting , Parents , Educational Status
2.
Viruses ; 14(3)2022 02 24.
Article in English | MEDLINE | ID: mdl-35336871

ABSTRACT

The human adenovirus type C5 (HAdV-C5) E1B-55K protein is a multifunctional regulator of HAdV-C5 replication, participating in many processes required for maximal virus production. Its multifunctional properties are primarily regulated by post-translational modifications (PTMs). The most influential E1B-55K PTMs are phosphorylation at highly conserved serine and threonine residues at the C-terminus, and SUMO conjugation to lysines 104 (K104) and 101 (K101) situated in the N-terminal region of the protein, which have been shown to regulate each other. Reversible SUMO conjugation provides a molecular switch that controls key functions of the viral protein, including intracellular trafficking and viral immune evasion. Interestingly, SUMOylation at SUMO conjugation site (SCS) K104 is negatively regulated by another multifunctional HAdV-C5 protein, E4orf6, which is known to form a complex with E1B-55K. To further evaluate the role of E4orf6 in the regulation of SUMO conjugation to E1B-55K, we analyzed different virus mutants expressing E1B-55K proteins with amino acid exchanges in both SCS (K101 and K104) in the presence or absence of E4orf6. We could exclude phosphorylation as factor for E4orf6-mediated reduction of E1B-55K SUMOylation. In fact, we demonstrate that a direct interaction between E1B-55K and E4orf6 is required to reduce E1B-55K SUMOylation. Additionally, we show that an E4orf6-mediated decrease of SUMO conjugation to K101 and K104 result in impaired co-localization of E1B-55K and SUMO in viral replication compartments. These findings indicate that E4orf6 inhibits E1B-55K SUMOylation, which could favor assembly of E4orf6-dependent E3 ubiquitin ligase complexes that are known to degrade a variety of host restriction factors by proteasomal degradation and, thereby, promote viral replication.


Subject(s)
Adenovirus Infections, Human , Adenoviruses, Human , Adenoviridae/metabolism , Adenovirus E1B Proteins/genetics , Adenovirus E1B Proteins/metabolism , Adenoviruses, Human/physiology , Humans , Sumoylation , Virus Replication
3.
Viruses ; 6(4): 1654-71, 2014 Apr 09.
Article in English | MEDLINE | ID: mdl-24721789

ABSTRACT

The host cell protein tetherin can restrict the release of enveloped viruses from infected cells. The HIV-1 protein Vpu counteracts tetherin by removing it from the site of viral budding, the plasma membrane, and this process depends on specific interactions between the transmembrane domains of Vpu and tetherin. In contrast, the glycoproteins (GPs) of two filoviruses, Ebola and Marburg virus, antagonize tetherin without reducing surface expression, and the domains in GP required for tetherin counteraction are unknown. Here, we show that filovirus GPs depend on the presence of their authentic transmembrane domains for virus-cell fusion and tetherin antagonism. However, conserved residues within the transmembrane domain were dispensable for membrane fusion and tetherin counteraction. Moreover, the insertion of the transmembrane domain into a heterologous viral GP, Lassa virus GPC, was not sufficient to confer tetherin antagonism to the recipient. Finally, mutation of conserved residues within the fusion peptide of Ebola virus GP inhibited virus-cell fusion but did not ablate tetherin counteraction, indicating that the fusion peptide and the ability of GP to drive host cell entry are not required for tetherin counteraction. These results suggest that the transmembrane domains of filoviral GPs contribute to tetherin antagonism but are not the sole determinants.


Subject(s)
Ebolavirus/physiology , Glycoproteins/metabolism , Host-Pathogen Interactions , Marburgvirus/physiology , Viral Proteins/metabolism , Antigens, CD , Cell Line , DNA Mutational Analysis , Ebolavirus/genetics , GPI-Linked Proteins/antagonists & inhibitors , Glycoproteins/genetics , Humans , Marburgvirus/genetics , Viral Proteins/genetics
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