complex(p(HGNC:FYN), p(HGNC:MAPT)) increases p(HGNC:MAPT, pmod(Ph))

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PubMed:19293145

FYN physically interacts with and phosphorylates tau protein, and the affinity of this physical interaction is enhanced in AD-associated mutations in tau protein (Bhaskar et al., 2005). Abeta rapidly induces tyrosine phosphorylation of many proteins (including tau protein) in human and cultured rat cortical neurons (Williamson et al., 2002). This phosphorylation is concomitant with phosphorylation and inactivation of focal adhesion kinase 1 (FADK1, a major downstream target of FYN), is blocked by inhibitors of SRC kinases and PI3K, and involves FYN associating physically with FADK1 (Williamson et al., 2002).

Related Edges 6

• a(CHEBI:"amyloid-beta") increases p(HGNC:MAPT, pmod(Ph, Tyr))
• p(HGNC:FYN) increases complex(p(HGNC:FYN), p(HGNC:PTK2))
• p(HGNC:MAPT, pmod(Ph, Tyr)) association p(HGNC:PTK2, pmod(Ph))
• p(HGNC:PTK2, pmod(Ph)) association p(HGNC:MAPT, pmod(Ph, Tyr))
• p(HGNC:PTK2, pmod(Ph)) decreases act(p(HGNC:PTK2))
• path(MESH:"Alzheimer Disease") increases complex(p(HGNC:FYN), p(HGNC:MAPT))

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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.

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