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Updated: Jan 31, 2026
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Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
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DjA1 maintains Golgi integrity via interaction with GRASP65
Jie Li1, Danming Tang1, Stephen C Ireland1
1Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1085.
Molecular Biology of the Cell
|December 20, 2018
Summary
The DnaJ homolog subfamily A member 1 (DjA1) protein binds to Golgi reassembly stacking protein of 65 kDa (GRASP65), promoting its oligomerization. This interaction is crucial for maintaining Golgi structure and function in mammalian cells.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The Golgi reassembly stacking protein of 65 kDa (GRASP65) is vital for Golgi stacking and ribbon linking via trans-oligomer formation.
- Understanding GRASP65 regulation is key to comprehending Golgi apparatus organization.
Purpose of the Study:
- To identify novel GRASP65-binding proteins and elucidate their role in Golgi structure.
- To investigate the functional significance of the interaction between DjA1 and GRASP65.
Main Methods:
- Biochemical methods to identify GRASP65-binding proteins.
- Cellular studies involving DjA1 depletion and Golgi reassembly assays.
- In vitro assays using purified proteins and cytosol.
Main Results:
- DnaJ homolog subfamily A member 1 (DjA1) was identified as a novel GRASP65-binding protein.
- Depletion of DjA1 caused Golgi fragmentation and impaired reassembly.
- DjA1 directly enhances GRASP65 oligomerization and Golgi membrane fusion, independent of its Hsc70 cochaperone activity.
Conclusions:
- DjA1 plays a critical role in maintaining Golgi structure and function.
- The interaction between DjA1 and GRASP65 promotes GRASP65 trans-oligomerization, essential for Golgi integrity.
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