RRC ID 18132
Author Shen J, Maruyama IN.
Title Nerve growth factor receptor TrkA exists as a preformed, yet inactive, dimer in living cells.
Journal FEBS Lett
Abstract The tropomyosin-related kinase A (TrkA) receptor and its ligand, nerve growth factor (NGF), play crucial roles in the development and function of the nervous system. NGF is believed to activate TrkA by bridging two TrkA monomers, leading to TrkA transphosphorylation. However, here we show that the majority of TrkA receptors exist as preformed, yet inactive, homodimers prior to NGF binding by using three different approaches such as chemical crosslinking and enzyme fragment complementation assay. Furthermore, TrkA homodimers are formed in endoplasmic reticulum before newly synthesized receptors reach the cell surface. These findings shed light on molecular mechanisms underlying transmembrane signaling by TrkA.
Volume 585(2)
Pages 295-9
Published 2011-1-21
DOI 10.1016/j.febslet.2010.12.031
PII S0014-5793(10)01026-4
PMID 21187090
MeSH Animals Cell Line Cell Membrane / metabolism Endoplasmic Reticulum / metabolism Humans Nerve Growth Factor / metabolism Protein Multimerization Protein Transport Rats Receptor, trkA / chemistry Receptor, trkA / metabolism* Receptors, Nerve Growth Factor / metabolism
IF 3.057
Times Cited 27
WOS Category BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
Resource
Human and Animal Cells PC-12(RCB0009) 293(RCB1637)