Autophosphorylation of PDGFRA extracellular domain dimers

Stable Identifier
R-HSA-9672173
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
Participants
Participates
Catalyst Activity

protein tyrosine kinase activity of extracellular domain mutant PDGFRA dimers [endoplasmic reticulum membrane]

Functional status

Gain of function of extracellular domain mutant PDGFRA dimers [endoplasmic reticulum membrane]

Disease Entity
Status
Disease
Name Identifier Synonyms
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
Authored
Reviewed
Created
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