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Inhibition of ADP‐ribosylation suppresses aberrant accumulation of lipidated apolipoprotein B in the endoplasmic reticulum
Author(s) -
Ohsaki Yuki,
Cheng Jinglei,
Yamairi Kazushi,
Pan Xiaoyue,
Hussain M. Mahmood,
Fujimoto Toyoshi
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.09.036
Subject(s) - endoplasmic reticulum , brefeldin a , apolipoprotein b , golgi apparatus , secretion , chemistry , microbiology and biotechnology , adp ribosylation factor , unfolded protein response , secretory pathway , biochemistry , cholesterol , biology
ApoB‐crescent, an endoplasmic reticulum (ER)‐lipid droplet amalgamation structure, is a useful marker to indicate aberrant lipidated apolipoprotein B accumulation in the hepatocyte ER. Blockade of the ER‐to‐Golgi transport by either vesicle transport inhibitors or dominant‐negative Arf1 caused a significant increase in ApoB‐crescents. However, a low concentration of Brefeldin A induced the same result without affecting protein secretion, suggesting ADP‐ribosylation as an additional mechanism. ADP‐ribosylation inhibitors not only suppressed the increase of ApoB‐crescents, but also rapidly dissolved existing ApoB‐crescents. These results implicate the involvement of ADP‐ribosylation in the ApoB‐crescent formation and maintenance process at the ER.