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Different subcellular localizations and functions of Arabidopsis myosin VIII
Year:
2008
Source of publication :
BMC Plant Biology
Authors :
אבו-עביד, מוחמד
;
.
בלאוסוב, אדוארד
;
.
גולומב, ליאור
;
.
שדות, עינת
;
.
Volume :
8
Co-Authors:
Golomb, L., Institute of Plant Sciences, Volcani Center, Bet-Dagan 50250, Israel
Abu-Abied, M., Institute of Plant Sciences, Volcani Center, Bet-Dagan 50250, Israel
Belausov, E., Institute of Plant Sciences, Volcani Center, Bet-Dagan 50250, Israel
Sadot, E., Institute of Plant Sciences, Volcani Center, Bet-Dagan 50250, Israel
Facilitators :
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0
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Total pages:
1
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Abstract:
Background. Myosins are actin-activated ATPases that use energy to generate force and move along actin filaments, dragging with their tails different cargos. Plant myosins belong to the group of unconventional myosins and Arabidopsis myosin VIII gene family contains four members: ATM1, ATM2, myosin VIIIA and myosin VIIIB. Results. In transgenic plants expressing GFP fusions with ATM1 (IQ-tail truncation, lacking the head domain), fluorescence was differentially distributed: while in epidermis cells at the root cap GFP-ATM1 equally distributed all over the cell, in epidermal cells right above this region it accumulated in dots. Further up, in cells of the elongation zone, GFP-ATM1 was preferentially positioned at the sides of transversal cell walls. Interestingly, the punctate pattern was insensitive to brefeldin A (BFA) while in some cells closer to the root cap, ATM1 was found in BFA bodies. With the use of different markers and transient expression in Nicotiana benthamiana leaves, it was found that myosin VIII co-localized to the plasmodesmata and ER, colocalized with internalized FM4-64, and partially overlapped with the endosomal markers ARA6, and rarely with ARA7 and FYVE. Motility of ARA6 labeled organelles was inhibited whenever associated with truncated ATM1 but motility of FYVE labeled organelles was inhibited only when associated with large excess of ATM1. Furthermore, GFP-ATM1 and RFP-ATM2 (IQ-tail domain) co-localized to the same spots on the plasma membrane, indicating a specific composition at these sites for myosin binding. Conclusion. Taken together, our data suggest that myosin VIII functions differently in different root cells and can be involved in different steps of endocytosis, BFA-sensitive and insensitive pathways, ER tethering and plasmodesmatal activity.
Note:
Related Files :
arabidopsis
brefeldin A
drug effect
Genetics
metabolism
multigene family
עוד תגיות
תוכן קשור
More details
DOI :
10.1186/1471-2229-8-3
Article number:
3
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
30064
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:51
Scientific Publication
Different subcellular localizations and functions of Arabidopsis myosin VIII
8
Golomb, L., Institute of Plant Sciences, Volcani Center, Bet-Dagan 50250, Israel
Abu-Abied, M., Institute of Plant Sciences, Volcani Center, Bet-Dagan 50250, Israel
Belausov, E., Institute of Plant Sciences, Volcani Center, Bet-Dagan 50250, Israel
Sadot, E., Institute of Plant Sciences, Volcani Center, Bet-Dagan 50250, Israel
Different subcellular localizations and functions of Arabidopsis myosin VIII
Background. Myosins are actin-activated ATPases that use energy to generate force and move along actin filaments, dragging with their tails different cargos. Plant myosins belong to the group of unconventional myosins and Arabidopsis myosin VIII gene family contains four members: ATM1, ATM2, myosin VIIIA and myosin VIIIB. Results. In transgenic plants expressing GFP fusions with ATM1 (IQ-tail truncation, lacking the head domain), fluorescence was differentially distributed: while in epidermis cells at the root cap GFP-ATM1 equally distributed all over the cell, in epidermal cells right above this region it accumulated in dots. Further up, in cells of the elongation zone, GFP-ATM1 was preferentially positioned at the sides of transversal cell walls. Interestingly, the punctate pattern was insensitive to brefeldin A (BFA) while in some cells closer to the root cap, ATM1 was found in BFA bodies. With the use of different markers and transient expression in Nicotiana benthamiana leaves, it was found that myosin VIII co-localized to the plasmodesmata and ER, colocalized with internalized FM4-64, and partially overlapped with the endosomal markers ARA6, and rarely with ARA7 and FYVE. Motility of ARA6 labeled organelles was inhibited whenever associated with truncated ATM1 but motility of FYVE labeled organelles was inhibited only when associated with large excess of ATM1. Furthermore, GFP-ATM1 and RFP-ATM2 (IQ-tail domain) co-localized to the same spots on the plasma membrane, indicating a specific composition at these sites for myosin binding. Conclusion. Taken together, our data suggest that myosin VIII functions differently in different root cells and can be involved in different steps of endocytosis, BFA-sensitive and insensitive pathways, ER tethering and plasmodesmatal activity.
Scientific Publication
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