Golgi complex beads in vertebrates and their relationship with clathrin coats.
Addition of tannic acid to the primary glutaraldehyde fixative and the viewing of thin sections by stereo electron microscopy greatly simplifies the detection of vertebrate cell Golgi complex beads which are otherwise difficult to see since they do not stain with bismuth. These results confirm the generality of conclusions from experiments on arthropod beads which are easily observed because of their bismuth affinity. In vertebrate and arthropod cells, bead rings encircle the base of forming transition vesicles below the growing portion of the vesicle that is covered with a clathrin coat. Their unique position at such a sharp functional and structural boundary in intercompartmental transport suggests that the bead rings may specify a select region of rough endoplasmic reticulum devoid of ribosomes where clathrin coats can induce transition vesicle formation and prevent intermixing of the elements of a returning transition vesicle.
D000818:Animals; D002966:Clathrin; D004721:Endoplasmic Reticulum / Q000648:ultrastructure; D005404:Fixatives; D006056:Golgi Apparatus / Q000648:ultrastructure*; D047348:Hydrolyzable Tannins; D007765:Lacrimal Apparatus / Q000648:ultrastructure; D007915:Lepidoptera / Q000648:ultrastructure*; D008297:Male; D008565:Membrane Proteins / Q000502:physiology*; D051379:Mice; D008854:Microscopy, Electron; D008954:Models, Biological; D009940:Organoids / Q000648:ultrastructure; D010179:Pancreas / Q000648:ultrastructure; D051381:Rats; D013194:Staining and Labeling; D013737:Testis / Q000648:ultrastructure
D002966:Clathrin; D005404:Fixatives; D047348:Hydrolyzable Tannins; D008565:Membrane Proteins