gamma-BAR, a novel AP-1-interacting protein involved in post-Golgi trafficking

2005 | journal article. A publication with affiliation to the University of Göttingen.

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​gamma-BAR, a novel AP-1-interacting protein involved in post-Golgi trafficking​
Neubrand, V. E.; Will, R. D.; Möbius, W. ; Poustka, A.; Wiemann, S.; Schu, P. V. & Dotti, C. G. et al.​ (2005) 
The EMBO Journal24(6) pp. 1122​-1133​.​ DOI: 

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Neubrand, V. E.; Will, R. D.; Möbius, Wiebke ; Poustka, Annemarie; Wiemann, Stefan; Schu, Peter Valentin; Dotti, C. G.; Pepperkok, R.; Simpson, Jeremy C.
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 gamma 1-adaptin at the trans-Golgi network (TGN) and on vesicular profiles. Overexpression of 2c18 increases the fraction of membrane-bound gamma 1-adaptin and inhibits its release from membranes in response to brefeldin A. Knockdown of 2c18 reduces the steady-state levels of gamma 1-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 gamma 1-adaptin is crucial for membrane association and thus the function of the AP-1 complex in living cells. We propose to name this protein gamma-BAR.
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The EMBO Journal 



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