| Literature DB >> 28777890 |
Xihua Yue1, Mengjing Bao1, Romain Christiano2, Siyang Li1,3,4, Jia Mei1, Lianhui Zhu1, Feifei Mao1, Qiang Yue1,3,4, Panpan Zhang1,3,4, Shuaiyang Jing1,3,4, James E Rothman1,5, Yi Qian1, Intaek Lee1.
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.Entities:
Keywords: ACBD3; Golgi; Golgin45; Rab-GTPase; membrane trafficking
Mesh:
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Year: 2017 PMID: 28777890 DOI: 10.1002/1873-3468.12780
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124