PTRN-1, a microtubule minus end-binding CAMSAP homolog, promotes microtubule function in Caenorhabditis elegans neurons

In neuronal processes, microtubules (MTs) provide structural support and serve as tracks for molecular motors. While it is known that neuronal MTs are more stable than MTs in non-neuronal cells, the molecular mechanisms underlying this stability are not fully understood. In this study, we used live...

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Bibliographic Details
Published in:eLife 2014-02, Vol.3, p.e01498
Main Authors: Richardson, Claire E, Spilker, Kerri A, Cueva, Juan G, Perrino, John, Goodman, Miriam B, Shen, Kang
Format: Article
Language:English
Subjects:
Animals
Axons
Caenorhabditis elegans - drug effects
Caenorhabditis elegans - genetics
Caenorhabditis elegans - metabolism
Caenorhabditis elegans Proteins - genetics
Caenorhabditis elegans Proteins - metabolism
Cell Biology
development
Drosophila melanogaster
Electron microscopy
Experiments
Genotype
Localization
MAP Kinase Kinase Kinases - metabolism
Microscopy
Microscopy, Electron
Microscopy, Fluorescence
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Microtubules
Microtubules - drug effects
Microtubules - metabolism
Molecular modelling
Morphology
Mutation
Neurites - metabolism
neuron
Neurons
Neurons - drug effects
Neurons - metabolism
Neuroscience
Phenotype
Polymerization
Proteins
Signal Transduction
Synaptic Vesicles - metabolism
Tubulin Modulators - pharmacology
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Summary:In neuronal processes, microtubules (MTs) provide structural support and serve as tracks for molecular motors. While it is known that neuronal MTs are more stable than MTs in non-neuronal cells, the molecular mechanisms underlying this stability are not fully understood. In this study, we used live fluorescence microscopy to show that the C. elegans CAMSAP protein PTRN-1 localizes to puncta along neuronal processes, stabilizes MT foci, and promotes MT polymerization in neurites. Electron microscopy revealed that ptrn-1 null mutants have fewer MTs and abnormal MT organization in the PLM neuron. Animals grown with a MT depolymerizing drug caused synthetic defects in neurite branching in the absence of ptrn-1 function, indicating that PTRN-1 promotes MT stability. Further, ptrn-1 null mutants exhibited aberrant neurite morphology and synaptic vesicle localization that is partially dependent on dlk-1. Our results suggest that PTRN-1 represents an important mechanism for promoting MT stability in neurons. DOI: http://dx.doi.org/10.7554/eLife.01498.001.
ISSN:2050-084X
2050-084X
DOI:10.7554/elife.01498