Restriction of docking protein to the rough endoplasmic reticulum: immunocytochemical localization in rat liver.
Docking protein (or SRP receptor) is an integral membrane protein essential for translocation of nascent polypeptides across the membrane of the endoplasmic reticulum (ER). Anti-docking protein antibodies were used to localize this protein in situ in thin frozen sections using protein A-gold detection methods. The majority of gold particles was restricted to ribosome-studded membranes, whereas particles were rarely seen in areas rich in smooth ER. Quantitative evaluation of labeling suggests that there is one molecule of docking protein for roughly 10 to 20 bound ribosomes. On the basis of these results we conclude that docking protein is the first functionally-characterized integral marker protein specific for the rough membranes of ER.
D000818:Animals; D003593:Cytoplasm / Q000648:ultrastructure; D004285:Dogs; D004721:Endoplasmic Reticulum / Q000032:analysis* / Q000648:ultrastructure; D005615:Freezing; D006046:Gold; D008099:Liver / Q000032:analysis* / Q000648:ultrastructure; D008565:Membrane Proteins / Q000032:analysis*; D008854:Microscopy, Electron; D008970:Molecular Weight; D011817:Rabbits; D051381:Rats
D008565:Membrane Proteins; C488952:Srpra protein, rat; D006046:Gold