ACBD 3 functions as a scaffold to organize the Golgi stacking proteins and a Rab33b‐ GAP
| Autor: | Feifei Mao, Jia Mei, Xihua Yue, Lianhui Zhu, Intaek Lee, Qiang Yue, James E. Rothman, Mengjing Bao, Romain Christiano, Yi Qian, Siyang Li, Panpan Zhang, Shuaiyang Jing |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
GTPase-activating protein Immunoblotting Vesicular Transport Proteins Biophysics Stacking Fluorescent Antibody Technique Golgi Apparatus Plasma protein binding Biology Biochemistry 03 medical and health sciences symbols.namesake Structural Biology Genetics Humans Molecular Biology Secretory pathway Adaptor Proteins Signal Transducing Microscopy Confocal GTPase-Activating Proteins Membrane Proteins Cell Biology Golgi apparatus Cell biology 030104 developmental biology Membrane protein rab GTP-Binding Proteins symbols HeLa Cells Protein Binding Binding domain |
| Zdroj: | FEBS Letters. 591:2793-2802 |
| ISSN: | 1873-3468 0014-5793 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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