The human docking protein does not associate with the membrane of the rough endoplasmic reticulum via a signal or insertion sequence-mediated mechanism.
Docking protein (DP, or SRP receptor) is an essential component of the cellular machinery that mediates the targeting of nascent secretory and membrane proteins to the rough endoplasmic reticulum (ER). In this study we have investigated the nature of its own targeting to its site of function, the rough ER. Using an in vitro transcription-translation system we demonstrate that DP is not inserted into the membrane via a classical SRP/DP-mediated process (in contrast to human ribophorins), nor via hydrophobic insertion sequences (in contrast to cytochrome b5). Instead, we suggest that membrane assembly of DP is receptor-mediated; requiring the presence in the membrane of other proteins that mediate its targeting and insertion.
Hortsch
M
M
European Molecular Biology Laboratory, Heidelberg, FRG.
Meyer
D I
DI
D000818:Animals; D004251:DNA Transposable Elements; D004285:Dogs; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D008565:Membrane Proteins / Q000096:biosynthesis* / Q000235:genetics; D008861:Microsomes / Q000378:metabolism; D014176:Protein Biosynthesis / Q000187:drug effects; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals; D012261:Ribonucleoproteins / Q000494:pharmacology; D018271:Signal Recognition Particle; D014158:Transcription, Genetic / Q000187:drug effects
D004251:DNA Transposable Elements; D008565:Membrane Proteins; D021382:Protein Sorting Signals; D012261:Ribonucleoproteins; C035026:SRPRA protein, human; D018271:Signal Recognition Particle