A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis
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- Title
- A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis
- Authors
- Jin, JB; Kim, YA; Kim, SJ; Lee, SH; Kim, DH; Cheong, GW; Hwang, I
- Date Issued
- 2001-07
- Publisher
- AMER SOC PLANT PHYSIOLOGISTS
- Abstract
- Dynamin, a high-molecular-weight GTPase, plays a critical role in vesicle formation at the plasma membrane during endocytosis in animal cells. Here we report the identification of a new dynamin homolog in Arabidopsis named Arabidopsis dynamin-like 6 (ADL6). ADL6 is quite similar to dynamin I in its structural organization: a conserved GTPase domain at the N terminus, a pleckstrin homology domain at the center, and a Pro-rich motif at the C terminus. In the cell, a majority of ADL6 is associated with membranes. Immunohistochemistry and in vivo targeting experiments revealed that ADL6 is localized to the Golgi apparatus. Expression of the dominant negative mutant ADL6[K51E] in Arabidopsis protoplasts inhibited trafficking of cargo proteins destined for the lytic vacuole and caused them to accumulate at the trans-Golgi network. In contrast, expression of ADL6[K51E] did not affect trafficking of a cargo protein, H+-ATPase:green fluorescent protein, destined for the plasma membrane. These results suggest that ADL6 is involved in vesicle formation for vacuolar trafficking at the trans-Golgi network but not for trafficking to the plasma membrane in plant cells.
- Keywords
- GTP-BINDING-PROTEIN; BREFELDIN-A; ENDOPLASMIC-RETICULUM; MOLECULAR-CLONING; PLANT-CELLS; SACCHAROMYCES-CEREVISIAE; SECRETORY PROTEINS; SORTING RECEPTOR; STORAGE PROTEINS; MAMMALIAN-CELLS
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/19469
- DOI
- 10.1105/tpc.13.7.1511
- ISSN
- 1040-4651
- Article Type
- Article
- Citation
- PLANT CELL, vol. 13, no. 7, page. 1511 - 1525, 2001-07
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