Publications by authors named "Avital Hacohen Lev-Ran"
Article Synopsis
- - The study investigates how GqPCR activation, typically associated with cell survival through the PI3K/AKT pathway, can instead trigger apoptosis in certain cells by inactivating AKT via a PP2Ac switch, a mechanism not fully understood prior.
- - Researchers identified Ser24 as a crucial phosphorylation site on PP2Ac, primarily regulated by classical PKCs, and demonstrated that altering this site (using S24A and S24E mutations) affects the activation and function of the PP2A switch leading to increased JNK-dependent apoptosis.
- - The findings suggest that targeting the PKC-mediated phosphorylation of Ser24-PP2Ac could offer new therapeutic strategies for treating specific cancers or endocrine disorders.
Retention of ERK in the cytoplasm mediates the pluripotency of embryonic stem cells.
Stem Cell Reports
January 2023
The dynamic subcellular localization of ERK1/2 plays an important role in regulating cell fate. Differentiation of mouse embryonic stem cells (mESCs) involves inductive stimulation of ERK1/2, and therefore, inhibitors of the ERK cascade are used to maintain pluripotency. Interestingly, we found that in pluripotent mESCs, ERK1/2 do not translocate to the nucleus either before or after stimulation.
View Article and Find Full Text PDFThe extracellular signal-regulated kinases 1/2 (ERK) are central signaling components that regulate stimulated cellular processes such as proliferation and differentiation. When dysregulated, these kinases participate in the induction and maintenance of various pathologies, primarily cancer. While ERK is localized in the cytoplasm of resting cells, many of its substrates are nuclear, and indeed, extracellular stimulation induces a rapid and robust nuclear translocation of ERK.
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