0000000000054753
AUTHOR
Cristina Maranto
Cellular stress induces cap-independent alpha-enolase/MBP-1 translation.
AbstractMyc promoter-binding protein-1 (MBP-1) is a shorter protein variant of the glycolytic enzyme alpha-enolase. Although several lines of evidence indicate that MBP-1 acts as a tumor suppressor, the cellular mechanisms and signaling pathways underlying MBP-1 expression still remain largely elusive. To dissect these pathways, we used the SkBr3 breast cancer cell line and non-tumorigenic HEK293T cells ectopically overexpressing alpha-enolase/MBP-1. Here, we demonstrate that induced cell stresses promote MBP-1 expression through the AKT/PERK/eIF2α signaling axis. Our results contribute to shedding light on the molecular mechanisms underlying MBP-1 expression in non-tumorigenic and cancer c…
Role of Enolase/MBP-1 in non-tumorigenic and cancer cells
The glycolytic enzyme α-enolase is a highly conserved protein involved in multiple functions (Díaz-Ramos A et al 2012). Besides the mainly cytoplasmic localization, the protein has been detected on the surface of prokaryotic and eukaryotic cells where it functions as a plasminogen receptor, while a shorter variant, called Myc promoter-binding protein-1 (MBP-1), is mainly located in the nucleus. Several lines of evidence indicate that MBP-1 acts as a tumor suppressor, negatively regulating cell proliferation or promoting apoptosis of cancer cells. Although a few reports indicate that stressful conditions, such as glucose deprivation or hypoxia, may modulate MBP-1 expression in mammalian cell…
Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface
AbstractCell surface expression of alpha-enolase, a glycolytic enzyme displaying moonlighting activities, has been shown to contribute to the motility and invasiveness of cancer cells through the protein non-enzymatic function of binding plasminogen and enhancing plasmin formation. Although a few recent records indicate the involvement of protein partners in the localization of alpha-enolase to the plasma membrane, the cellular mechanisms underlying surface exposure remain largely elusive. Searching for novel interactors and signalling pathways, we used low-metastatic breast cancer cells, a doxorubicin-resistant counterpart and a non-tumourigenic mammary epithelial cell line. Here, we demon…