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Journal Article

Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane.

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Görlich,  D.
Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Vogel, F., Hartmann, E., Görlich, D., & Rapoport, T. A. (1990). Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane. European Journal of Cell Biology, 53(2), 197-202.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0015-3BB1-A
Abstract
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.