AMPK is required for recovery from metabolic stress induced by ultrasound microbubble treatment

Lo, Louis; Uchenunu, Oro; Botelho, Roberto J.; Antonescu, Costin N.; Karshafian, Raffi

doi:10.1016/j.isci.2022.105883

Cited by 5 publications

(2 citation statements)

References 63 publications

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“…To resolve whether these conditions triggered an increase in cell death in any of the conditions examined, we quantified the CellTox Green positive objects and normalized this to the cell confluence in each image ( Figure 7D , right panels ), as we have done previously 52 . This allows the measurement of cell death indexed to a measure of total cell abundance.…”

Section: Resultsmentioning

confidence: 99%

“…Cell abundance and non-viable cells were measured using an Incucyte SX5 environmentally controlled microscope as previously described 52 . Following induction of construct expression with doxycycline for 24h, MDA-MB-231 cells were placed in full media or EBSS supplemented with 10 ng/mL EGF, and also further supplemented with CellTox CellTox Green Cytotoxicity Assay reagent (Promega G8741) by adding 1µL of the dye in 10mL of media.…”

Section: Methodsmentioning

confidence: 99%

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Control of GSK3β nuclear localization by amino acid signaling requires GATOR1 but is mTORC1-independent

Schwendener Forkel,

Ibazebo,

Soha

et al. 2024

Preprint

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The availability of certain amino acids regulates cell survival, proliferation, growth, differentiation, and other cellular functions. Sensing of amino acids that converges on the GATOR1 and GATOR2 complexes supports activation of mTORC1 during amino acid replete conditions. Whether amino acid-derived cues regulate additional pathways remains poorly understood. We uncover that amino acid sensing involving GATOR1 and GATOR2 regulates the cellular localization of glycogen synthase kinase 3beta (GSK3beta). GATOR1 is required to recruit a subset of GSK3beta to the lysosome selectively in the presence of amino acids. In addition, while under nutrient replete conditions GSK3beta is largely cytosolic, amino acid starvation drives a portion of GSK3beta into the nucleus. Acute replenishment of specific amino acids in starved cells triggered nuclear exit of GSK3beta. This amino acid-stimulated GSK3beta nuclear exit required GATOR1 and GATOR2 but was independent of mTORC1 and its activating RagA/B GTPases. This suggests that GATOR1 has a function that diverges from control of mTORC1 to regulate the nucleocytoplasmic shuttling of GSK3beta. Furthermore, experimental restriction of GSK3beta to the cytoplasm decreased cell survival in amino acid deficient conditions. This suggests that control of GSK3beta nuclear localization by GATOR-dependent signals represents a cellular adaptation to metabolic stress that supports cell survival.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Control of GSK3β nuclear localization by amino acid signaling requires GATOR1 but is mTORC1-independent

Schwendener Forkel,

Ibazebo,

Soha

et al. 2024

Preprint

View full text Add to dashboard Cite

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Versatile function of AMPK signaling in osteosarcoma: An old player with new emerging carcinogenic functions

Hashemi,

Razzazan,

Bagheri

et al. 2023

Pathology - Research and Practice

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HER2 expression defines unique requirements for flotillin and c-Src in EGFR signaling

Abousawan

Orofiamma

Fairn

et al. 2023

Journal of Cell Science

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The epidermal growth factor receptor (EGFR) controls many cellular functions. Upon binding its ligand, the receptor undergoes dimerization, phosphorylation, and activation of signals including the phosphatidylinositol-3-kinase (PI3K)-Akt pathway. While some studies indicated that EGFR signaling may be controlled by signal enrichment within various membrane rafts such as flotillin nanodomains, others have found a limited effect of disruption of these nanodomains on EGFR signaling, suggesting that specific factor(s) may define context-specific control of EGFR signaling. Ligand-bound EGFR can homodimerize, or instead undergo heterodimerization with the related receptor HER2 when the latter is expressed. We examined how EGFR signaling in the presence of HER2 distinctly requires flotillin nanodomains. Induction of HER2 expression altered EGFR signaling duration consistent with EGFR/HER2 heterodimer formation. EGFR and c-Src localized within plasma membrane structures demarked by flotillin-1 more prominently in HER2-expressing cells. Consistently, HER2-expressing cells, but not cells lacking HER2, were dependent on flotillin-1 and c-Src for EGFR signaling leading to Akt activation and cell proliferation. Hence, HER2 expression establishes a requirement of EGFR signaling for flotillin membrane rafts and c-Src.

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AMPK is required for recovery from metabolic stress induced by ultrasound microbubble treatment

Cited by 5 publications

References 63 publications

Control of GSK3β nuclear localization by amino acid signaling requires GATOR1 but is mTORC1-independent

Control of GSK3β nuclear localization by amino acid signaling requires GATOR1 but is mTORC1-independent

Versatile function of AMPK signaling in osteosarcoma: An old player with new emerging carcinogenic functions

HER2 expression defines unique requirements for flotillin and c-Src in EGFR signaling

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