PDGFR-alpha and STMN1 cooperate to exacerbate cytotoxic effects of vinblastine (Mus musculus)
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Description
Stathmin (SMTMN1) normally binds to alpha-beta tubulin heterodimers, but this process is negatively regulated by phosphorylation. In this way phosphorylated Stathmin indirectly promotes polymerization. PDGFRα dephosphorylates STMN1, which leads to increased tubulin depolymerization. Vinblastine inhibits polymerization, effectively resulting in depolymerization. During mitosis, this triggers the defense mechanism "spindle assembly checkpoint" (SAC), which and results in either apoptosis or mitotic slippage.
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- Jun HJ, Appleman VA, Wu HJ, Rose CM, Pineda JJ, Yeo AT, Delcuze B, Lee C, Gyuris A, Zhu H, Woolfenden S, Bronisz A, Nakano I, Chiocca EA, Bronson RT, Ligon KL, Sarkaria JN, Gygi SP, Michor F, Mitchison TJ, Charest A; ''A PDGFRα-driven mouse model of glioblastoma reveals a stathmin1-mediated mechanism of sensitivity to vinblastine.''; Nat Commun, 2018 PubMed Europe PMC Scholia
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External references
DataNodes
| Name | Type | Database reference | Comment |
|---|---|---|---|
| Pdgfra | GeneProduct | ENSMUSG00000029231 (Ensembl)  | |
| Stmn1 | GeneProduct | ENSMUSG00000028832 (Ensembl) | |
| Vinblastine | Metabolite | CHEBI:27375 (ChEBI) |
Annotated Interactions
No annotated interactions
