Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane.
The signal sequence receptor (SSR), an integral membrane glycoprotein of 34 kDa, has previously been shown to be a component of the molecular environment which nascent polypeptide chains meet in passage through the endoplasmic reticulum (ER) membrane. We have used antibodies directed against the SSR and both immunocytochemistry and cell fractionation to determine its distribution in rat liver cells. SSR was found largely restricted to the rough ER. Only small amounts of the protein were detected in smooth ER. These results provide further evidence for a functional differentiation of rough and smooth ER and for a role of SSR in protein translocation across the ER membrane.
Vogel
F
F
Zentralinstitut für Molekularbiologie, Akademie der Wissenschaften, Berlin-Buch/Federal Republic of Germany.
Hartmann
E
E
Görlich
D
D
Rapoport
T A
TA
D000818:Animals; D002458:Cell Fractionation; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure; D007150:Immunohistochemistry; D007425:Intracellular Membranes / Q000378:metabolism* / Q000648:ultrastructure; D008099:Liver / Q000166:cytology / Q000378:metabolism*; D008854:Microscopy, Electron; D008862:Microsomes, Liver / Q000378:metabolism / Q000648:ultrastructure; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism*; D018160:Receptors, Cytoplasmic and Nuclear; D018000:Receptors, Peptide
D011956:Receptors, Cell Surface; D018160:Receptors, Cytoplasmic and Nuclear; D018000:Receptors, Peptide; C036318:signal peptide receptor