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  • Title: Organization and dynamics of microtubules in Torpedo marmorata electrocyte: selective association with specialized domains of the postsynaptic membrane.
    Author: Jasmin BJ, Changeux JP, Cartaud J.
    Journal: Neuroscience; 1991; 43(1):151-62. PubMed ID: 1922764.
    Abstract:
    The distribution and subcellular organization of two components of the secretory pathway, the Golgi apparatus and microtubules, have been investigated in Torpedo marmorata electrocyte. This highly polarized syncytium, embryologically derived from skeletal muscle cells, displays distinct plasma membrane domains on its innervated and non-innervated faces, and it played a critical role in the identification of the acetylcholine receptor. By immunocytochemical analysis, we show that in the electrocyte, numerous focal Golgi bodies are dispersed throughout the cytoplasm in frequent association with nuclei. Under experimental conditions known to stabilize microtubules, we reveal an elaborate network composed of two populations of microtubules exhibiting different dynamic properties as evaluated by cold-stability, resistance to nocodazole and post-translational modification. This network appears organized from several nucleating centers located in the medial plane of the cell that are devoided of centrioles. The network displays an asymmetric distribution with individual microtubules converging towards the troughs of the postsynaptic membrane folds. In these particular regions, we consistently observed clusters of non-coated vesicles in association with the microtubules. The organization of the microtubules in the electrocyte may thus result in a functional polarization of the cytoplasm. In other polarized cells, the particular organization of the secretory pathway accounts for the intracellular routing of membrane proteins. The organization that we have observed in the electrocyte may thus lead to the vectorial delivery of synaptic proteins to the innervated plasma membrane. Furthermore, the abundance of synaptic proteins makes the electrocyte a unique model with which to decipher the mechanisms involved in the sorting and targeting of these glycoproteins.
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