The prenylated rab GTPase receptor PRA1.F4 contributes to protein exit from the golgi apparatus
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SCOPUS
- Title
- The prenylated rab GTPase receptor PRA1.F4 contributes to protein exit from the golgi apparatus
- Authors
- Lee, M.H.; Yoo, Y.-J.; Kim, D.H.; Hanh, N.H.; Kwon, Y.; Hwang, I.
- Date Issued
- 2017-07
- Publisher
- American Society of Plant Biologists
- Abstract
- Prenylated Rab acceptor1 (PRA1) functions in the recruitment of prenylated Rab proteins to their cognate organelles. Arabidopsis (Arabidopsis thaliana) contains a large number of proteins belonging to the AtPRA1 family. However, their physiological roles remain largely unknown. Here, we investigated the physiological role of AtPRA1.F4, a member of the AtPRA1 family. A T-DNA insertion knockdown mutant of AtPRA1.F4, atpra1.f4, was smaller in stature than parent plants and possessed shorter roots, whereas transgenic plants overexpressing HA:AtPRA1.F4 showed enhanced development of secondary roots and root hairs. However, both overexpression and knockdown plants exhibited increased sensitivity to high-salt stress, lower vacuolar Na+/K+-ATPase and plasma membrane ATPase activities, lower and higher pH in the vacuole and apoplast, respectively, and highly vesiculated Golgi apparatus. HA:AtPRA1.F4 localized to the Golgi apparatus and assembled into high-molecular-weight complexes. atpra1.f4 plants displayed a defect in vacuolar trafficking, which was complemented by low but not high levels of HA:AtPRA1.F4. Overexpression of HA:AtPRA1.F4 also inhibited protein trafficking at the Golgi apparatus, albeit differentially depending on the final destination or type of protein: trafficking of vacuolar proteins, plasma membrane proteins, and trans-Golgi network (TGN)-localized SYP61 was strongly inhibited; trafficking of TGN-localized SYP51 was slightly inhibited; and trafficking of secretory proteins and TGN-localized SYP41 was negligibly or not significantly inhibited. Based on these results, we propose that Golgi-localized AtPRA1.F4 is involved in the exit of many but not all types of post-Golgi proteins from the Golgi apparatus. Additionally, an appropriate level of AtPRA1.F4 is crucial for its function at the Golgi apparatus. ? 2017 American Society of Plant Biologists. All rights reserved.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/51002
- DOI
- 10.1104/pp.17.00466
- ISSN
- 0032-0889
- Article Type
- Article
- Citation
- Plant Physiology, vol. 174, no. 3, page. 1576 - 1594, 2017-07
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