English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Background  In 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.    Results  In 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 AtGRIP aa711–753 , AtGRIP aa711–766  and AtGRIP aa711–776  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.    Conclusions  These 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.

The C-TERMINUS of AtGRIP Is Crucial for Its Self-Association and for Targeting to Golgi Stacks in Arabidopsis