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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2000-10-13
pubmed:abstractText
Neurotrophin (NT) signals may be moved from axon terminals to neuron cell bodies via signaling endosomes-organelles in which NTs continue to be bound to their activated receptors. Suggesting that clathrin-coated membranes serve as one source of signaling endosomes, in earlier studies we showed that nerve growth factor (NGF) treatment increased clathrin at the plasma membrane and resulted in colocalization of clathrin with TrkA, the receptor tyrosine kinase for NGF. Strikingly, however, we also noted that most clathrin puncta at the surface of NGF-treated cells did not colocalize with TrkA, raising the possibility that NGF induces a general increase in clathrin-coated membrane formation. To explore this possibility further, we examined the distribution of clathrin in NGF- and BDNF-treated cells. NGF signaling in PC12 cells robustly redistributed the adaptor protein AP2 and the clathrin heavy chain (CHC) to surface membranes. Using confocal and epifluorescence microscopy, as well as biochemical assays, we showed the redistribution of clathrin to be attributable to the activation of TrkA. Significantly, NGF signaled through TrkA to induce an increase in clathrin-mediated membrane trafficking, as revealed in the increased endocytosis of transferrin. In that BDNF treatment increased AP2 and clathrin at the surface membranes of hippocampal neurons, these findings may represent a physiologically significant response to NTs. We conclude that NT signaling increases clathrin-coated membrane formation and clathrin-mediated membrane trafficking and speculate that this effect contributes to their trophic actions via the increased internalization of receptors and other proteins that are present in clathrin-coated membranes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7325-33
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11007890-Adaptor Protein Complex 2, pubmed-meshheading:11007890-Adaptor Protein Complex alpha Subunits, pubmed-meshheading:11007890-Adaptor Proteins, Vesicular Transport, pubmed-meshheading:11007890-Animals, pubmed-meshheading:11007890-Brain-Derived Neurotrophic Factor, pubmed-meshheading:11007890-Cell Membrane, pubmed-meshheading:11007890-Cells, Cultured, pubmed-meshheading:11007890-Clathrin, pubmed-meshheading:11007890-Clathrin Heavy Chains, pubmed-meshheading:11007890-Endocytosis, pubmed-meshheading:11007890-Hippocampus, pubmed-meshheading:11007890-Humans, pubmed-meshheading:11007890-Membrane Proteins, pubmed-meshheading:11007890-Mice, pubmed-meshheading:11007890-Nerve Growth Factor, pubmed-meshheading:11007890-Neurons, pubmed-meshheading:11007890-PC12 Cells, pubmed-meshheading:11007890-Phosphorylation, pubmed-meshheading:11007890-Rats, pubmed-meshheading:11007890-Rats, Sprague-Dawley, pubmed-meshheading:11007890-Receptor, trkA, pubmed-meshheading:11007890-Signal Transduction
pubmed:year
2000
pubmed:articleTitle
NGF signals through TrkA to increase clathrin at the plasma membrane and enhance clathrin-mediated membrane trafficking.
pubmed:affiliation
Department of Physiology, University of California at San Francisco, San Francisco, California 94143, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't