Premium
ACBD 3 functions as a scaffold to organize the Golgi stacking proteins and a Rab33b‐ GAP
Author(s) -
Yue Xihua,
Bao Mengjing,
Christiano Romain,
Li Siyang,
Mei Jia,
Zhu Lianhui,
Mao Feifei,
Yue Qiang,
Zhang Panpan,
Jing Shuaiyang,
Rothman James E.,
Qian Yi,
Lee Intaek
Publication year - 2017
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 - 10.1002/1873-3468.12780
Subject(s) - stacking , golgi apparatus , scaffold protein , chemistry , microbiology and biotechnology , scaffold , biophysics , biochemistry , biology , engineering , biomedical engineering , signal transduction , organic chemistry , cell
Golgin45 plays important roles in Golgi stack assembly and is known to bind both the Golgi stacking protein GRASP 55 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 ( ACBD 3) is likely to be a novel binding partner of Golgin45. ACBD 3 interacts with Golgin45 via its GOLD domain, while its co‐expression significantly increases Golgin45 targeting to the Golgi. Furthermore, ACBD 3 recruits TBC 1D22, a Rab33b GTP ase activating protein ( GAP ), to a large multi‐protein complex containing Golgin45 and GRASP 55. These results suggest that ACBD 3 may provide a scaffolding to organize the Golgi stacking proteins and a Rab33b‐ GAP at the medial‐Golgi.