@misc{10481/86543,
year = {2005},
url = {https://hdl.handle.net/10481/86543},
abstract = {A novel peripheral membrane protein (2c18) that interacts directly with the gamma ‘ear’ domain of the adaptor protein complex 1 (AP-1) in vitro and in vivo is described. Ultrastructural analysis demonstrates a colocalization of 2c18 and c1-adaptin at the trans-Golgi network (TGN) and on vesicular profiles. Overexpression of 2c18 increases the fraction of membrane-bound c1-adaptin and inhibits its release from membranes in response to brefeldin A. Knockdown of 2c18 reduces the steady-state levels of c1-adaptin on membranes. Overexpression or downregulation of 2c18 leads to an increased secretion of the lysosomal hydrolase cathepsin D, which is sorted by the mannose-6-phosphate receptor at the TGN, which itself involves AP-1 function for trafficking between the TGN and endosomes. This suggests that the direct interaction of 2c18 and c1-adaptin is crucial for membrane association and thus the function of the AP-1 complex in living cells. We propose to name this protein c-BAR.},
publisher = {EMBO Press},
keywords = {AP-1},
keywords = {Gamma-adaptin},
title = {gamma-BAR, a novel AP-1-interacting protein involved in post-Golgi trafficking},
doi = {10.1038/ sj.emboj.7600600},
author = {Neubrand, Veronika Elisabeth and Will, Rainer D and Möbius, Wiebke and Poustka, Annemarie and Wiemann, Stefan and Schu, Peter and Dotti, Carlos G and Pepperkok, Rainer and Simpson, Jeremy C},
}