Amphiphysin 2 and members of the BAR-domain family of proteins participate in a wide array of cellular processes including cell cycle and endocytosis. Given that amphiphysin 2 is related to diverse cell responses as a result of metabolic stress, we investigated in macrophages whether oxidative stress originated by the internalization of oxidized low density lipoproteins (oxLDL) affect both, the expression of amphiphysin 2 and its binding partner c-Myc. Here we report that under oxidative stress, a complex formation between amphiphysin 2(Bin1) and c-Myc allows the cell to develop a novel survival equilibrium state established between cell proliferation and cell death. We propose that under conditions of oxidative stress given by the internalization of oxLDL, macrophages employ the formation of the amphiphysin 2(Bin1)/c-Myc complex as a control mechanism to initially avoid the process of cell death in an attempt to prolong cell survival.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.bbrc.2018.09.121DOI Listing

Publication Analysis

Top Keywords

formation amphiphysin
12
oxidative stress
12
cell
8
cell survival
8
cell death
8
amphiphysin
6
survival regulation
4
regulation receptor-mediated
4
receptor-mediated endocytosis
4
endocytosis chemically-modified
4

Similar Publications

Bin/Amphiphysin/Rvs (BAR) domains are highly conserved domains found in all eukaryotes. BAR domain proteins form crescent-shaped dimers that sense and sculpt curved lipid membranes and play key roles in various cellular processes. However, their functions in mammalian development are poorly understood.

View Article and Find Full Text PDF

Characterization of atypical BAR domain-containing proteins coded by Toxoplasma gondii.

J Biol Chem

December 2024

Université Côte d'Azur, CNRS, INSERM, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France. Electronic address:

Article Synopsis
  • * The study identifies and characterizes TgREMIND and TgBAR2, two proteins with BAR domains that play key roles in the creation of essential organelles and vesicular trafficking in the parasite.
  • * TgREMIND can bind to and remodel membranes, while TgBAR2 uniquely deforms anionic membranes, highlighting their differing roles in the parasite's membrane dynamics and trafficking system.
View Article and Find Full Text PDF

Endocytosis plays a complex role in pathogen-host interactions. It serves as a pathway for pathogens to enter the host cell and acts as a part of the immune defense mechanism. Endocytosis involves the formation of lipid membrane vesicles and the reshaping of the cell membrane, a task predominantly managed by proteins containing BAR (Bin1/Amphiphysin/yeast RVS167) domains.

View Article and Find Full Text PDF

The Nedd4L ubiquitin ligase is activated by FCHO2-generated membrane curvature.

EMBO J

December 2024

Department of Molecular Pharmacology, Faculty of Life Sciences, Kumamoto University, 1-1-1 Honjyo, Kumamoto, 860-8556, Japan.

The C2-WW-HECT domain ubiquitin ligase Nedd4L regulates membrane sorting during endocytosis through the ubiquitination of cargo molecules such as the epithelial sodium channel (ENaC). Nedd4L is catalytically autoinhibited by an intramolecular interaction between its C2 and HECT domains, but the protein's activation mechanism is poorly understood. Here, we show that Nedd4L activation is linked to membrane shape by FCHO2, a Bin-Amphiphysin-Rsv (BAR) domain protein that regulates endocytosis.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!