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Entity

Name
cellular response to stress
Namespace
go
Namespace Version
20180921
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/go-names.belns

Appears in Networks 5

In-Edges 2

bp(GO:"ubiquitin-dependent protein catabolic process") regulates bp(GO:"cellular response to stress") View Subject | View Object

Ubiquitin-mediated proteolysis of a variety of cellular proteins plays an important role in many basic cellular processes. Among these are regulation of cell cycle and division, differentiation and development, involvement in the cellular response to stress and extracellular effectors, morphogenesis of neuronal networks, modulation of cell surface receptors, ion channels and the secretory pathway, DNA repair, transcriptional regulation, transcriptional silencing, long-term memory, circadian rhythms, regulation of the immune and inflammatory responses,and biogenesis of organelles PubMed:14556719

p(HGNC:HSF1) regulates bp(GO:"cellular response to stress") View Subject | View Object

For exam- ple, small molecules (e.g., geldanamycin) that activate heat shock factor 1, the main transcrip- tional regulator of the cytosolic stress response, increase the effective concentration of cytosolic chaperones and suppress the aggregation of various disease proteins (8, 38, 228–230). PubMed:23746257

Out-Edges 5

bp(GO:"cellular response to stress") increases a(MESH:"Heat-Shock Proteins") View Subject | View Object

Several members of the chaperone family are upregulated in response to stress and, thus, these factors have been termed heat shock proteins (Hsps) PubMed:21882945

bp(GO:"cellular response to stress") increases a(HBP:"Hsp27 oligomers") View Subject | View Object

These proteins are ATP-independent chaperones that undergo homo-oligomerization in response to stress [97,98] PubMed:21882945

bp(GO:"cellular response to stress") increases tloc(p(HGNC:TFEB), fromLoc(GO:cytosol), toLoc(GO:nucleus)) View Subject | View Object

Under starvation or stress, TFEB translocates to the nucleus and binds the CRE element to promote expression of macroautophagy and lysosomal genes [88]. PubMed:29758300

bp(GO:"cellular response to stress") increases complex(p(HGNC:TFEB), p(INTERPRO:"cAMP response element binding (CREB) protein")) View Subject | View Object

Under starvation or stress, TFEB translocates to the nucleus and binds the CRE element to promote expression of macroautophagy and lysosomal genes [88]. PubMed:29758300

bp(GO:"cellular response to stress") increases p(HGNC:SQSTM1) View Subject | View Object

Cellular stresses such as polyQ expression, proteasome impairment, oxidative stress, and increased misfolded protein burden activate transcription and translation of p62, suggesting that it functions broadly in stress situations [83,84] PubMed:18930136

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.