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Signaling by cytosolic PDGFRA and PDGFRB fusion proteins

Summary

Organism

Homo sapiens (human)

Reactome

R-HSA-9673766

PubChem

R-HSA-9673766

Description

In addition to activating missense mutations and in-frame deletions, PDGFRA and PDGFRB are also subject to gene fusion events arising from chromosomal rearrangements. PDGFR fusions often consist of the cytosolic domain of the receptor tyrosine kinase fused to the N-terminal oligomerization domain of an intracellular protein, leading to ligand-independent dimerization and constitutive activation (reviewed in Wang et al, 2016; Appiah-Kubi et al, 2017). To date there are about 35 identified PDGFR fusion partners, most of which form fusions with PDGFRB (reviewed in Appiah-Kubi et al, 2017). The most common cytosolic fusion partners of PDGFRA is FIP1L1, an RNA processing factor (Cools et al, 2003; Stover et al, 2006; Simon et al, 2008; Andrae et al, 2008; Ozawa et al, 2010; Appiah-Kubi et al, 2017). Fusion partners with PDGFRB are numerous but occurrence of these proteins is rare (Hidalgo-Curtis et al, 2010; reviewed in Wang et al, 2016; Appiah-Kubi et al, 2017).

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SPV: a JavaScript Signaling Pathway Visualizer, Bioinformatics, 2018

Displaying 1 entry
UniProt ID	Protein Name	Gene Symbol	Pathway Viewer
Q6UN15	Pre-mRNA 3'-end-processing factor FIP1	FIP1 FIP1L1 RHE	view

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