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FEBS Lett. 2017 Aug 4. doi: 10.1002/1873-3468.12780. [Epub ahead of print]

ACBD3 functions as a scaffold to organize the Golgi stacking proteins and a Rab33b-GAP.

Yue X1, Bao M1, Christiano R2, Li S1,3,4, Mei J1, Zhu L1, Mao F1, Yue Q1,3,4, Zhang P1,3,4, Jing S1,3,4, Rothman JE1,5, Qian Y1, Lee I1.

Author information

1
Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, China.
2
Department of Genetics and Complex Diseases, School of Public Health, Harvard medical school, Boston, MA, USA.
3
Institute of Biochemistry and Cell Biology, Shanghai, China.
4
University of Chinese Academy of Sciences, Shanghai, China.
5
Department of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.

Abstract

Golgin45 plays important roles in Golgi stack assembly and is known to bind both the Golgi stacking protein GRASP55 and Rab2 in the medial-Golgi cisternae. In this study, we sought to further characterize the cisternal adhesion complex using a proteomics approach. We report here that Acyl-CoA binding domain containing 3 (ACBD3) is likely to be a novel binding partner of Golgin45. ACBD3 interacts with Golgin45 via its GOLD domain, while its co-expression significantly increases Golgin45 targeting to the Golgi. Furthermore, ACBD3 recruits TBC1D22, a Rab33b GTPase activating protein (GAP), to a large multi-protein complex containing Golgin45 and GRASP55. These results suggest that ACBD3 may provide a scaffolding to organize the Golgi stacking proteins and a Rab33b-GAP at the medial-Golgi.

KEYWORDS:

ACBD3; Golgi; Golgin45; Rab-GTPase; membrane trafficking

PMID:
28777890
DOI:
10.1002/1873-3468.12780
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