Structural basis of the transmembrane domain dimerization and rotation in the activation mechanism of the TRKA receptor by nerve growth factor.
brain derived neurotrophic factor (BDNF)
nerve growth factor (NGF)
neurotrophin
nuclear magnetic resonance (NMR)
p75 neurotrophin receptor
receptor tyrosine kinase
transmembrane domain
tropomyosin receptor kinase A (TRKA)
tropomyosin receptor kinase B (TRKB)
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
03 01 2020
03 01 2020
Historique:
received:
01
10
2019
revised:
26
11
2019
pubmed:
6
12
2019
medline:
9
9
2020
entrez:
6
12
2019
Statut:
ppublish
Résumé
Tropomyosin-receptor kinases (TRKs) are essential for the development of the nervous system. The molecular mechanism of TRKA activation by its ligand nerve growth factor (NGF) is still unsolved. Recent results indicate that at endogenous levels most of TRKA is in a monomer-dimer equilibrium and that the binding of NGF induces an increase of the dimeric and oligomeric forms of this receptor. An unsolved issue is the role of the TRKA transmembrane domain (TMD) in the dimerization of TRKA and the structural details of the TMD in the active dimer receptor. Here, we found that the TRKA-TMD can form dimers, identified the structural determinants of the dimer interface in the active receptor, and validated this interface through site-directed mutagenesis together with functional and cell differentiation studies. Using
Identifiants
pubmed: 31801826
pii: S0021-9258(17)49566-4
doi: 10.1074/jbc.RA119.011312
pmc: PMC6952603
pii:
doi:
Substances chimiques
Nerve Growth Factor
9061-61-4
Receptor, trkA
EC 2.7.10.1
Banques de données
PDB
['2n90', '2IFG']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
275-286Informations de copyright
© 2020 Franco et al.
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