Autophosphorylation of PDGFRA extracellular domain dimers

Stable Identifier
Reaction [transition]
Homo sapiens
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Constitutively active extracellular domain mutants of PDGFRA are trans-autophosphorylated at internal compartments in the absence of stimulation by ligand (Clarke and Dirks, 2003; Ozawa et al, 2010; Paugh et al 2013; Ip et al, 2018).

Literature References
PubMed ID Title Journal Year
12569364 A human brain tumor-derived PDGFR-alpha deletion mutant is transforming

Clarke, ID, Dirks, PB

Oncogene 2003
30389923 Neomorphic PDGFRA extracellular domain driver mutations are resistant to PDGFRA targeted therapies

Ip, CKM, Ng, PKS, Jeong, KJ, Shao, SH, Ju, Z, Leonard, PG, Hua, X, Vellano, CP, Woessner, R, Sahni, N, Scott, KL, Mills, GB

Nat Commun 2018
20889717 PDGFRA gene rearrangements are frequent genetic events in PDGFRA-amplified glioblastomas

Ozawa, T, Brennan, CW, Wang, L, Squatrito, M, Sasayama, T, Nakada, M, Huse, JT, Pedraza, A, Utsuki, S, Yasui, Y, Tandon, A, Fomchenko, EI, Oka, H, Levine, RL, Fujii, K, Ladanyi, M, Holland, EC

Genes Dev. 2010
23970477 Novel oncogenic PDGFRA mutations in pediatric high-grade gliomas

Paugh, BS, Zhu, X, Qu, C, Endersby, R, Diaz, AK, Zhang, J, Bax, DA, Carvalho, D, Reis, RM, Onar-Thomas, A, Broniscer, A, Wetmore, C, Zhang, J, Jones, C, Ellison, DW, Baker, SJ

Cancer Res. 2013
Participant Of
Catalyst Activity
Catalyst Activity
protein tyrosine kinase activity of extracellular domain mutant PDGFRA dimers [endoplasmic reticulum membrane]
Physical Entity
Name Identifier Synonyms
cancer 162 malignant tumor, malignant neoplasm, primary cancer
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