RET dimerizes

Stable Identifier
Homo sapiens
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It is widely accepted that RET undergoes dimerization and transphosphorylation following Glial cell line-derived neurotrophic factor (GDNF) binding to the GDNF-family receptor:RET complex. Transphosphorylation of specific tyrosine residues is a prerequisite for activation of RET tyrosine kinase activity and downstream signaling (Santoro et al. 1995, Airaksinen et al. 1999, Takeda et al. 2001, Leppänen et al. 2004). However, self-association of RET in the absence of GDNF has been reported and may contribute to the mechanism of RET activation (Kjaer et al. 2006). The stoichiometry and kinetics of ligand-receptor complex formation are not well understood. It is assumed that all GDNF family of ligands (GFL) members interact with their cognate co-receptor and activate RET in a similar manner to GDNF (Airaksinen & Saarma 2002).

Literature References
PubMed ID Title Journal Year
11491658 Osmotic stress-mediated activation of RET kinases involves intracellular disulfide-bonded dimer formation

Takeda, K, Kato, M, Wu, J, Iwashita, T, Suzuki, H, Takahashi, M, Nakashima, I

Antioxid. Redox Signal. 2001
15044950 The structure of GFRalpha1 domain 3 reveals new insights into GDNF binding and RET activation

Leppänen, VM, Bespalov, MM, Runeberg-Roos, P, Puurand, U, Merits, A, Saarma, M, Goldman, A

EMBO J. 2004
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Orthologous Events