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.
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http://dx.doi.org/10.1016/j.bbrc.2018.09.121 | DOI Listing |
Life Sci Alliance
February 2025
Molecular and Cellular Biology Graduate Program, Stony Brook University, Stony Brook, NY, USA
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 PDFEur Neuropsychopharmacol
January 2025
Department of Psychiatry and Psychotherapy, Medical Center - University of Freiburg, Faculty of Medicine, University of Freiburg, Freiburg, Germany. Electronic address:
J Biol Chem
December 2024
Université Côte d'Azur, CNRS, INSERM, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France. Electronic address:
Pathogens
October 2024
Department of Chemistry & Chemical Biology, The University of New Mexico, Albuquerque, NM 87131, USA.
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 PDFEMBO 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.
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