Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-2-22
pubmed:abstractText
Nerve growth factor (NGF) initiates its trophic effects by long-range signaling through binding, internalization, and transport of a ligand-receptor complex from the axon terminal to the cell body. However, the mechanism by which retrograde transport of NGF takes place has not been elucidated. Here we describe an interaction between the Trk receptor tyrosine kinase and a 14 kDa light chain of cytoplasmic dynein. After transfection in human embryonic kidney 293 cells, this 14 kDa dynein light chain was found to bind to TrkA, TrkB, and TrkC receptors. Mapping experiments indicated that the 14 kDa dynein light chain binds to the distal region of the TrkA juxtamembrane domain. Coimmunoprecipitation experiments in vivo indicate that Trk receptors are in a complex with the 14 kDa light chain and 74 kDa intermediate chain of dynein. Confirming the physiological relevance of this association, a marked accumulation of Trk with the 14 kDa and the 74 kDa dynein components was observed after ligation of the sciatic nerve. The association of Trk receptors with components of cytoplasmic dynein suggests that transport of neurotrophins during vesicular trafficking may occur through a direct interaction of the Trk receptor with the dynein motor machinery.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
RC125
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11157096-Animals, pubmed-meshheading:11157096-Cells, Cultured, pubmed-meshheading:11157096-Cytoplasm, pubmed-meshheading:11157096-Humans, pubmed-meshheading:11157096-Kidney, pubmed-meshheading:11157096-Ligation, pubmed-meshheading:11157096-Microtubule Proteins, pubmed-meshheading:11157096-Microtubule-Associated Proteins, pubmed-meshheading:11157096-Molecular Motor Proteins, pubmed-meshheading:11157096-Mutagenesis, Site-Directed, pubmed-meshheading:11157096-Neurons, pubmed-meshheading:11157096-Nuclear Proteins, pubmed-meshheading:11157096-Precipitin Tests, pubmed-meshheading:11157096-Protein Binding, pubmed-meshheading:11157096-Rats, pubmed-meshheading:11157096-Receptor, trkA, pubmed-meshheading:11157096-Recombinant Fusion Proteins, pubmed-meshheading:11157096-Sciatic Nerve, pubmed-meshheading:11157096-Sequence Deletion, pubmed-meshheading:11157096-Transfection, pubmed-meshheading:11157096-Two-Hybrid System Techniques, pubmed-meshheading:11157096-t-Complex Genome Region
pubmed:year
2001
pubmed:articleTitle
Association of Trk neurotrophin receptors with components of the cytoplasmic dynein motor.
pubmed:affiliation
Molecular Neurobiology Program, Skirball Institute for Biomolecular Medicine, Departments of Cell Biology , New York, New York 10016, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't