Abstract
BackgroundIn animals and fungi, dimerization is crucial for targeting GRIP domain proteins to the Golgi apparatus. Only one gene in the Arabidopsis genome, AtGRIP, codes for a GRIP domain protein. It remains unclear whether AtGRIP has properties similar to those of GRIP domain proteins.ResultsIn this study, western blot and yeast two-hybrid analyses indicated that AtGRIPs could form a parallel homodimer. In addition, yeast two-hybrid analysis indicated that AtGRIPaa711–753, AtGRIPaa711–766 and AtGRIPaa711–776 did not interact with themselves, but the intact GRIP domain with the AtGRIP C-terminus did. Confocal microscopy showed that only an intact GRIP domain with an AtGRIP C-terminus could localize to the Golgi stacks in Arabidopsis leaf protoplasts. A BLAST analysis showed that the C-terminus of GRIP proteins was conserved in the plant kingdom. Mutagenesis and yeast two-hybrid analyses showed that the L742 of AtGRIP contributed to dimerization and was crucial for Golgi localization.ConclusionsThese results indicate that the C-terminus of GRIP proteins is essential for self-association and for targeting of Golgi stacks in plant cells. We suggest that several properties of GRIP proteins differ between plant and animal cells.
Highlights
The Golgi apparatus consists of a series of dynamically stacked cisternae and plays a key role in glycoprotein modification and processing along with vesicle classification and secretion in eukaryotic cells
We suggest that the C-terminus of GRIP is essential for its dimerization and for targeting to Golgi stacks in plant cells, which is not consistent with known data on GRIP proteins in animal cells
We confirmed that the mutation of L742 to alanine disrupted AtGRIP dimerization and abolished its Golgi targeting. These results demonstrate that L742 is crucial for AtGRIP dimerization, and this dimerization is essential for the Golgi targeting of GRIP domain proteins in plant cells
Summary
The Golgi apparatus consists of a series of dynamically stacked cisternae and plays a key role in glycoprotein modification and processing along with vesicle classification and secretion in eukaryotic cells. Previous reports indicated that GRIP domain proteins play an important role in maintaining the structural and functional stability of the TGN in animal cells, and alterations in the levels of these proteins could induce structural abnormalities and/or disturb the membrane transport pathway in the TGN [12,13,14]. One gene in the Arabidopsis genome, AtGRIP, codes for a GRIP domain protein It remains unclear whether AtGRIP has properties similar to those of GRIP domain proteins
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