Publications by authors named "Aleksandra Janowicz"
Background: Endoplasmic reticulum (ER) stress is a hallmark of neurodegenerative diseases such as multiple sclerosis (MS). However, this physiological mechanism has multiple manifestations that range from impaired clearance of unfolded proteins to altered mitochondrial dynamics and apoptosis. While connections between the triggering of the unfolded protein response (UPR) and downstream mitochondrial dysfunction are poorly understood, the membranous contacts between the ER and mitochondria, called the mitochondria-associated membrane (MAM), could provide a functional link between these two mechanisms.
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- The palmitoylation of calnexin enhances its presence in the mitochondria-associated membrane (MAM) and affects its functional roles.
- Palmitoylated calnexin interacts with SERCA 2b to regulate calcium content and signaling between the endoplasmic reticulum (ER) and mitochondria, while non-palmitoylated calnexin interacts with ERp57 for quality control functions.
- During ER stress, calnexin's palmitoylation decreases, leading to a functional shift from calcium regulation to protein chaperoning and adjusting its location within the ER.
ALG-2 is a highly conserved calcium binding protein in the cytoplasm which belongs to the family of penta-EF hand proteins. Recently, we showed that ALG-2 is interacting with RBM22, a highly conserved spliceosomal nuclear protein (Montaville et al. Biochim.
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