Phosphatidylserine-binding protein lactadherin inhibits protein translocation across the ER membrane.

Hitoshi Yamamoto, Yuichiro Kida, Masao Sakaguchi

Graduate School of Life Science, University of Hyogo, Kouto 3-2-1 Ako-gun, Hyogo 678-1297, Japan.

Biochemical and biophysical research communications 2013 May 10

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Secretory and membrane proteins are translocated across and inserted into the endoplasmic reticulum membrane via translocon channels. To investigate the effect of the negatively-charged phospholipid phosphatidylserine on the translocation of nascent polypeptide chains through the translocon, we used the phosphatidylserine-binding protein lactadherin C2-domain. Lactadherin inhibited targeting of nascent chain to the translocon by signal sequence and the initiation of translocation. Moreover, lactadherin inhibited the movement of the translocating polypeptide chain regardless of the presence or absence of positively-charged residues. Phosphatidylserine might be critically involved in translocon function, but it is not a major determinant for translocation arrest of positively-charged residues. Copyright © 2013 Elsevier Inc. All rights reserved.

Citation

Hitoshi Yamamoto, Yuichiro Kida, Masao Sakaguchi. Phosphatidylserine-binding protein lactadherin inhibits protein translocation across the ER membrane. Biochemical and biophysical research communications. 2013 May 10;434(3):620-6