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Open Access Research article

Sec61β, a subunit of the Sec61 protein translocation channel at the Endoplasmic Reticulum, is involved in the transport of Gurken to the plasma membrane.

Anshuman Kelkar12* and Bernhard Dobberstein1

Author Affiliations

1 Zentrum für Molekulare Biologie Universitat Heidelberg, Im Neuenheimer Feld 282, Heidelberg 69120, Germany

2 The Rockefeller University and Howard Hughes Medical Institute, 1230 York Avenue, New York, NY 10065, USA

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BMC Cell Biology 2009, 10:11  doi:10.1186/1471-2121-10-11

Published: 18 February 2009



Protein translocation across the membrane of the Endoplasmic Reticulum (ER) is the first step in the biogenesis of secretory and membrane proteins. Proteins enter the ER by the Sec61 translocon, a proteinaceous channel composed of three subunits, α, β and γ. While it is known that Sec61α forms the actual channel, the function of the other two subunits remains to be characterized.


In the present study we have investigated the function of Sec61β in Drosophila melanogaster. We describe its role in the plasma membrane traffic of Gurken, the ligand for the Epidermal Growth Factor (EGF) receptor in the oocyte. Germline clones of the mutant allele of Sec61β show normal translocation of Gurken into the ER and transport to the Golgi complex, but further traffic to the plasma membrane is impeded. The defect in plasma membrane traffic due to absence of Sec61β is specific for Gurken and is not due to a general trafficking defect.


Based on our study we conclude that Sec61β, which is part of the ER protein translocation channel affects a post-ER step during Gurken trafficking to the plasma membrane. We propose an additional role of Sec61β beyond protein translocation into the ER.