Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Appears in Networks 2

In-Edges 8

bp(GO:"proteasomal protein catabolic process") decreases deg(p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356))) View Subject | View Object

Tau phosphorylated at Ser262 or Ser356 cannot be recognized by the C terminus of HSP70‑interacting protein–heat shock protein 90 (CHIP–HSP90) complex and is thus spared from proteasomal degradation PubMed:26631930

p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) decreases deg(p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356))) View Subject | View Object

Tau phosphorylated at Ser262 or Ser356 cannot be recognized by the C terminus of HSP70‑interacting protein–heat shock protein 90 (CHIP–HSP90) complex and is thus spared from proteasomal degradation PubMed:26631930

a(CHEBI:epoxomicin) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) View Subject | View Object

Missorted dendritic MAPT showed phosphorylation mainly at the 12E8 sites upon treatment with either the autophagy inhibitor wortmannin (Fig. 4B; 57.2±9.4% dendrites) or the proteasomal inhibitor epoxomicin (Fig. 4C, 62.9±7.4% dendrites) (Fig. 4A-C, quantification in Fig. 4D), but not at the AT8 and the PHF1 (p-S396/p-S404) sites (Fig. S5, Fig 4D). PubMed:30145931

a(CHEBI:wortmannin) positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) View Subject | View Object

Missorted dendritic MAPT showed phosphorylation mainly at the 12E8 sites upon treatment with either the autophagy inhibitor wortmannin (Fig. 4B; 57.2±9.4% dendrites) or the proteasomal inhibitor epoxomicin (Fig. 4C, 62.9±7.4% dendrites) (Fig. 4A-C, quantification in Fig. 4D), but not at the AT8 and the PHF1 (p-S396/p-S404) sites (Fig. S5, Fig 4D). PubMed:30145931

a(HBP:"amyloid-beta oligomers") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

bp(GO:autophagy) increases deg(p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356))) View Subject | View Object

Thus, the dendritic and axonal MAPT are differentially phosphorylated. Based on this observation, we can conclude that the dendritic MAPT degraded by autophagy or proteasomal pathways is phosphorylated mainly at the 12E8 site. PubMed:30145931

act(p(FPLX:Proteasome)) increases deg(p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356))) View Subject | View Object

Thus, the dendritic and axonal MAPT are differentially phosphorylated. Based on this observation, we can conclude that the dendritic MAPT degraded by autophagy or proteasomal pathways is phosphorylated mainly at the 12E8 site. PubMed:30145931

Out-Edges 5

p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) decreases complex(p(HGNC:MAPT), p(HGNC:STUB1)) View Subject | View Object

Tau phosphorylated at Ser262 or Ser356 cannot be recognized by the C terminus of HSP70‑interacting protein–heat shock protein 90 (CHIP–HSP90) complex and is thus spared from proteasomal degradation PubMed:26631930

p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) decreases deg(p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356))) View Subject | View Object

Tau phosphorylated at Ser262 or Ser356 cannot be recognized by the C terminus of HSP70‑interacting protein–heat shock protein 90 (CHIP–HSP90) complex and is thus spared from proteasomal degradation PubMed:26631930

p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) positiveCorrelation a(HBP:"amyloid-beta oligomers") View Subject | View Object

In addition, it has been reported that in cultured neurons, Aβ oligomers induce MAPT missorting into the somatodendritic compartment, and the missorted MAPT is phosphorylated mainly at the 12E8 (p-S262/p-S356) and AT8 (p-S202/p-T205) sites [6]. PubMed:30145931

p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) positiveCorrelation a(CHEBI:wortmannin) View Subject | View Object

Missorted dendritic MAPT showed phosphorylation mainly at the 12E8 sites upon treatment with either the autophagy inhibitor wortmannin (Fig. 4B; 57.2±9.4% dendrites) or the proteasomal inhibitor epoxomicin (Fig. 4C, 62.9±7.4% dendrites) (Fig. 4A-C, quantification in Fig. 4D), but not at the AT8 and the PHF1 (p-S396/p-S404) sites (Fig. S5, Fig 4D). PubMed:30145931

p(HGNC:MAPT, pmod(Ph, Ser, 262), pmod(Ph, Ser, 356)) positiveCorrelation a(CHEBI:epoxomicin) View Subject | View Object

Missorted dendritic MAPT showed phosphorylation mainly at the 12E8 sites upon treatment with either the autophagy inhibitor wortmannin (Fig. 4B; 57.2±9.4% dendrites) or the proteasomal inhibitor epoxomicin (Fig. 4C, 62.9±7.4% dendrites) (Fig. 4A-C, quantification in Fig. 4D), but not at the AT8 and the PHF1 (p-S396/p-S404) sites (Fig. S5, Fig 4D). PubMed:30145931

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.