Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2005-4-12
pubmed:abstractText
Axonal transport is required for the elaboration and maintenance of synaptic morphology and function. Liprin-alphas are scaffolding proteins important for synapse structure and electrophysiology. A reported interaction with Kinesin-3 (Kif1a) suggested Liprin-alpha may also be involved in axonal transport. Here, at the light and ultrastructural levels, we discover aberrant accumulations of synaptic vesicle markers (Synaptotagmin and Synaptobrevin-GFP) and clear-core vesicles along Drosophila Liprin-alpha mutant axons. Analysis of presynaptic markers reveals reduced levels at Liprin-alpha synapses. Direct visualization of Synaptobrevin-GFP transport in living animals demonstrates a decrease in anterograde processivity in Liprin-alpha mutants but also an increase in retrograde transport initiation. Pull-down assays reveal that Liprin-alpha interacts with Drosophila Kinesin-1 (Khc) but not dynein. Together, these findings suggest that Liprin-alpha promotes the delivery of synaptic material by a direct increase in kinesin processivity and an indirect suppression of dynein activation. This work is the first to use live observation in Drosophila mutants to demonstrate the role of a scaffolding protein in the regulation of bidirectional transport. It suggests the synaptic strength and morphology defects linked to Liprin-alpha may in part be due to a failure in the delivery of synaptic-vesicle precursors.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase, http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Kinesin, http://linkedlifedata.com/resource/pubmed/chemical/Liprin-alpha protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmins
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0960-9822
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
684-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15823543-Animals, pubmed-meshheading:15823543-Axonal Transport, pubmed-meshheading:15823543-Calcium-Binding Proteins, pubmed-meshheading:15823543-Drosophila Proteins, pubmed-meshheading:15823543-Drosophila melanogaster, pubmed-meshheading:15823543-Glutathione Transferase, pubmed-meshheading:15823543-Green Fluorescent Proteins, pubmed-meshheading:15823543-Kinesin, pubmed-meshheading:15823543-Membrane Glycoproteins, pubmed-meshheading:15823543-Membrane Proteins, pubmed-meshheading:15823543-Microscopy, Electron, pubmed-meshheading:15823543-Nerve Tissue Proteins, pubmed-meshheading:15823543-Phosphoproteins, pubmed-meshheading:15823543-R-SNARE Proteins, pubmed-meshheading:15823543-Synapses, pubmed-meshheading:15823543-Synaptic Vesicles, pubmed-meshheading:15823543-Synaptotagmins
pubmed:year
2005
pubmed:articleTitle
Direct observation demonstrates that Liprin-alpha is required for trafficking of synaptic vesicles.
pubmed:affiliation
Department of Cell Biology and Program in Neuroscience, Harvard Medical School, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural