14-3-3 proteins at the crossroads of neurodevelopment and schizophrenia

Antunes, André Saraiva Leão Marcelo; Saia-Cereda, Verônica M.; Crunfli, Fernanda; Martins‐de‐Souza, Daniel

doi:10.1080/15622975.2021.1925585

Cited by 4 publications

(3 citation statements)

References 186 publications

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“…Moreover, we detected acetylated 14-3-3 gamma in this pathway. By regulating their targets, 14-3-3 proteins play a role in neurogenesis, neuronal migration and differentiation, synaptogenesis and dopamine synthesis ( Antunes et al, 2022 ). The biological relevance of acetylation has been investigated in some 14-3-3 isoforms ( Choudhary et al, 2009 ; Aghazadeh et al, 2014 ; Frontini-Lopez et al, 2021 ); however, we identified different acetylated site on 14-3-3 gamma.…”

Section: Discussionmentioning

confidence: 99%

Chronic exercise remodels the lysine acetylome in the mouse hippocampus

Qian

Zhang

et al. 2022

Front. Mol. Neurosci.

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Physical exercise benefits hippocampal function through various molecular mechanisms. Protein acetylation, a conserved and widespread post-translational modification, is involved in the synaptic plasticity and memory. However, whether exercise can change global acetylation and the role of acetylated proteins in the hippocampus have remained largely unknown. Herein, using healthy adult mice running for 6 weeks as exercise model and sedentary mice as control, we analyzed the hippocampal lysine acetylome and proteome by Liquid chromatography-tandem mass spectrometry. As a result, we profiled the lysine acetylation landscape for the hippocampus and identified 3,876 acetyl sites and 1,764 acetylated proteins. A total of 272 acetyl sites on 252 proteins were differentially regulated by chronic exercise, among which 18.58% acetylated proteins were annotated in mitochondria. These proteins were dominantly deacetylated and mainly associated with carbon-related metabolism, the Hippo signaling pathway, ribosomes, and protein processing. Meanwhile, 21 proteins were significantly expressed and enriched in the pathway of complement and coagulation cascades. Our findings provide a new avenue for understanding the molecular mechanisms underlying the benefits of exercise for hippocampal function and can contribute to the promotion of public health.

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Section: Discussionmentioning

confidence: 99%

Chronic exercise remodels the lysine acetylome in the mouse hippocampus

Qian

Zhang

et al. 2022

Front. Mol. Neurosci.

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“…Based on the design and our results, it is presumed that TDPP could have great degradation efficiency for proteins with those three kinds of motifs. While 14-3-3 and P-14-3-3-BME proteins are involved in many cellular events, including neural development (Antunes et al, 2022), cancer proliferation and apoptosis (Aljabal and Yap, 2020; Huang et al, 2020; Yang et al, 2020), autoimmune disorder (McGowan et al, 2020), virus infection (Liu et al, 2021), etc., the TDPP-induced degradation could be significant in regulating the related downstream pathways and biological events.…”

Section: Discussionmentioning

confidence: 99%

A ubiquitination-mediated degradation system to target phospho-14-3-3-binding-motif embedded proteins

Huang

et al. 2022

Preprint

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The phosphorylation of 14-3-3 binding motif is involved in many cellular processes. A strategy that enables targeted degradation of phospho-14-3-3-binding-motif embedded (P-14-3-3-BME) proteins for studying their functions is highly desirable for basic research. Here, we report a phosphorylation-induced, ubiquitin-proteasome-system-mediated targeted protein degradation (TPD) strategy that allows specific degradation of P-14-3-3-BME proteins. Specifically, by ligating a modified von Hippel-Lindau E3-ligase with an engineered 14-3-3 bait, we generated a protein chimera referred to as Targeted Degradation of P-14-3-3-BME Protein (TDPP). TDPP can serve as a universal degrader for P-14-3-3-BME proteins based on the specific recognition of the phosphorylation in 14-3-3 binding motifs. TDPP shows high efficiency and specificity to a difopein-EGFP reporter, general and specific P-14-3-3-BME proteins. TDPP can also be applied for the validation of P-14-3-3-BME proteins. These results strongly support TDPP as a powerful tool for 14-3-3 related research.

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“…14-3-3 proteins are a highly conserved, ubiquitously expressed family of proteins, including seven known isoforms in mammalian species (β, γ, ε, η, δ, τ, ζ). These proteins associate with many intracellular proteins involved in a variety of cellular processes including regulation of the cell cycle, metabolism and protein trafficking [35][36][37]. The 14-3-3 protein provides a functional basis site for binding to target proteins by forming a homodimer or heterodimer, consequently, acting as molecular chaperone or intermediate [38].…”

Section: Identification Of 14-3-3 Isoforms Expressed In Fertilized Mo...mentioning

confidence: 99%

Ser149 is another potential 14-3-3 ε binding site of Cdc25B in the G2/M transition of mouse fertilized eggs

Pang

Hou

et al. 2023

Preprint

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Cell cycle division 25B (CDC25B) belongs to the family of cell cycle regulatory proteins. It drives G2/M transition by activating cyclin-dependent protein kinases (CDK1), also known as CDC2, whose activity is directly related to its subcellular localization and phosphorylation state.14-3-3 (YHWA) regulates cell division cycle by binding to Cdc25B as a chaperone protein in mammals. Previously, we found that Cdc25B- Ser149 plays an important role in G2/M transition of mouse fertilized eggs, but the molecular mechanism of this transition remains unclear. In this study, we assessed the role of 14-3-3 epsilon (YHWAE) interaction with phosphorylated Cdc25B-Ser149 in G2/M transition of mouse fertilized eggs. Co-expression of Cdc25B-S149A and 14-3-3 epsilon could effectively activate maturation promoting factor (MPF) through direct dephosphorylation of Cdc2-Tyr15, and induce G2 fertilized eggs to enter mitosis rapidly. However, co-expression of the phosphomimic Cdc25B-S149D or Cdc25B-WT and 14-3-3 epsilon showed no significant difference in comparison with control groups. 14-3-3 epsilon binds to Cdc25B-WT, which is abolished when Ser149 is mutated to Ala. In addition, we found that 14-3-3 epsilon and Cdc25B were co-localized in the cytoplasm at the G1, S and early G2 phases. Cdc25B was translocated from the cytoplasm to the nucleus at the late G2 phase. However, when Ser149 is mutated to Ala, the cytoplasmic localization of Cdc25B is completely abolished. Our findings suggest that Cdc25B-Ser149 is another specific binding site for 14-3-3 epsilon in G2/M transition of one-cell fertilized mouse eggs, which plays essential roles in the regulation of early development of fertilized mouse eggs.

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14-3-3 proteins at the crossroads of neurodevelopment and schizophrenia

Cited by 4 publications

References 186 publications

Chronic exercise remodels the lysine acetylome in the mouse hippocampus

Chronic exercise remodels the lysine acetylome in the mouse hippocampus

A ubiquitination-mediated degradation system to target phospho-14-3-3-binding-motif embedded proteins

Ser149 is another potential 14-3-3 ε binding site of Cdc25B in the G2/M transition of mouse fertilized eggs

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