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Metabolomicsp53 regulates Chaperone-mediated autophagy

p53 protects against the initiation and progression of a plethora of cancers, but the mechanisms underlying this critical function remain incompletely understood. In addition, chaperone-mediated autophagy (CMA) is major form of autophagy unique to vertebrates, yet both its regulation and function...

2026-10-03 | MTBLS13190 | MetaboLights
ProteomicsStarvation-induced Hsc70 O-GlcNAcylation activates chaperone-mediated autophagy
O-linked β-N-acetylglucosamine (O-GlcNAc) functions as a nutrition rheostat to mediate cellular signaling pathways. It fluctuates in response to various nutritional factors, for instance, glucose. Previous investigations have shown that both glucose surplus and glucose deprivation upregulate O-GlcNA...
ORGANISM(S): Homo sapiens (Human) 
2026-06-29 | PXD070146 | Pride
Hsc70  o-glcnac  chaperone-mediated autophagy  ataxin-10  ogt 
GenomicsTranscriptomic data of downregulated chaperone-mediated autophagy in glioma stem cell activity.
Transcriptomic data of downregulated chaperone-mediated autophagy in glioma stem cell activity.
PRJNA752577 | ENA
ProteomicsChaperone-mediated autophagy supports organ regeneration and fibroblast quiescence in mouse models of fibrosis
Chaperone-mediated autophagy (CMA) acting as a crucial, selective protein degradation pathway is a key topic in understanding tissue remodeling and disease, with recent research showing its pivotal role in maintaining organ health, particularly through the maintenance of fibroblast quiescence and su...
ORGANISM(S): Mus Musculus 
2026-01-22 | PXD073386 |
GenomicsProgrammable targeted RNA degradation via dCas13d-directed chaperone-mediated autophagy (dCasCMA)
Programmable targeted RNA degradation via dCas13d-directed chaperone-mediated autophagy (dCasCMA)
PRJNA1249926 | ENA
ProteomicsO-GlcNAcase SUMOylation studies identify the SUMO-code in chaperone-mediated autophagy
O-GlcNAcase (OGA) is the sole eraser for the intracellular O-linked N-acetylglucosamine (O-GlcNAc). OGA has many roles in diverse processes, such as cancer and embryonic stem cells, but its exact regulating mechanism is far from understood. Herein we studied small ubiquitin-like modifier (SUMO) modi...
ORGANISM(S): Homo Sapiens 
PXD056772 |
ProteomicsTargeting chaperone-mediated autophagy inhibits properties of glioblastoma stem cells and restores anti-tumor immunity
Chaperone-mediated autophagy (CMA), a selective autophagic process, plays a crucial role in maintaining intracellular quality and facilitating cellular responses to stress. While CMA has been implicated in finely regulating the stemness of normal stem cells, its significance in cancer stem cells (CS...
ORGANISM(S): Homo sapiens (Human) 
2025-09-22 | PXD060464 | Pride
Mst4 Chaperone-mediated autophagy Gsc Lamp2a Gbm 
ProteomicsActivation of autophagy depends on Atg1/ULK1 mediated phosphorylation of the chaperone Hsp90
The molecular chaperone Hsp90 is involved in the stability and activity of its client proteins which largely comprise of kinases. Phosphorylation of Hsp90 by these kinase clients provides a reciprocal regulatory mechanism between these proteins, however the mechanism of regulating the cellular pathw...
ORGANISM(S): Homo sapiens (Human) 
2023-09-08 | PXD038924 | Pride
Heat shock protein-90 (hsp90) Co-chaperone Serine/threonine protein phosphatase-5 (pp5) Sumoylation Molecular chaperone Phosphorylation 
ProteomicsChaperone-mediated autophagy maintains glioma stem cell activity controlling different proteomic and transcriptomic pathways (U251)
Chaperone-mediated autophagy (CMA) is a homeostatic process essential for the lysosomal degradation of individual proteins. CMA activity directly depends on the levels of LAMP2A, critical receptor at the lysosomal membrane, to which CMA substrate proteins are bound. In glioblastoma (GBM), the most c...
ORGANISM(S): Homo sapiens (Human) 
2022-08-02 | PXD029393 | Pride
Glioblastoma Chaperone-mediated autophagy Lamp2a Label free 
ProteomicsO-GlcNAcylation stabilizes ULK1 by inhibiting chaperone-mediated autophagy upon HPV infection
Human papillomaviruses (HPVs) are conducive to a fraction of head and neck squamous cell carcinoma (HNSCC). Previously we demonstrated that HPV16 oncogene E6 or E6/E7 transduction increases the abundance of O-linked GlcNAcylation (O-GlcNAc) transferase (OGT). Herein we focus on the effects of O-GlcN...
ORGANISM(S): Homo sapiens (Human) 
2022-10-14 | PXD031095 | Pride
O-glcnac  ulk1  hpv  hnscc  macroautophagy  chaperone-mediated autophagy 
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