Profilin promotes formin-mediated actin filament assembly and vesicle transport during polarity formation in pollen. Issue 4 (8th February 2021)
- Record Type:
- Journal Article
- Title:
- Profilin promotes formin-mediated actin filament assembly and vesicle transport during polarity formation in pollen. Issue 4 (8th February 2021)
- Main Title:
- Profilin promotes formin-mediated actin filament assembly and vesicle transport during polarity formation in pollen
- Authors:
- Liu, Chang
Zhang, Yi
Ren, Haiyun - Abstract:
- Abstract: Pollen germination is critical for the reproduction of flowering plants. Formin-dependent actin polymerization plays vital roles in vesicle trafficking and polarity establishment during this process. However, how formin-mediated actin assembly is regulated in vivo remains poorly understood. Here, we investigated the function of reproductive profilin 4 and 5 (PRF4 and PRF5) in polarity establishment during pollen germination in Arabidopsis thaliana . Our data showed that the actin filament content was reduced in the prf4 prf5 double mutant and substantially increased in both PRF4- and PRF5-overexpressing pollen grains. By contrast, the positive effect of profilin in promoting actin polymerization was abolished in a formin mutant, atfh5 . In addition, the interaction between Arabidopsis formin homology 5 (AtFH5) and actin filaments was attenuated and the trafficking of AtFH5-labeled vesicles was slowed in prf4 prf5 pollen grains. Formation of the collar-like structure at the germination pore was also defective in prf4 prf5 pollen grains as the fast assembly of actin filaments was impaired. Together, our results suggest that PRF4 and PRF5 regulate vesicle trafficking and polarity establishment during pollen germination by promoting AtFH5-mediated actin polymerization and enhancing the interaction between AtFH5 and actin filaments. Abstract : Profilin enhances the interaction between formin and actin, which assists formin with rapid actin polymerization and thereforeAbstract: Pollen germination is critical for the reproduction of flowering plants. Formin-dependent actin polymerization plays vital roles in vesicle trafficking and polarity establishment during this process. However, how formin-mediated actin assembly is regulated in vivo remains poorly understood. Here, we investigated the function of reproductive profilin 4 and 5 (PRF4 and PRF5) in polarity establishment during pollen germination in Arabidopsis thaliana . Our data showed that the actin filament content was reduced in the prf4 prf5 double mutant and substantially increased in both PRF4- and PRF5-overexpressing pollen grains. By contrast, the positive effect of profilin in promoting actin polymerization was abolished in a formin mutant, atfh5 . In addition, the interaction between Arabidopsis formin homology 5 (AtFH5) and actin filaments was attenuated and the trafficking of AtFH5-labeled vesicles was slowed in prf4 prf5 pollen grains. Formation of the collar-like structure at the germination pore was also defective in prf4 prf5 pollen grains as the fast assembly of actin filaments was impaired. Together, our results suggest that PRF4 and PRF5 regulate vesicle trafficking and polarity establishment during pollen germination by promoting AtFH5-mediated actin polymerization and enhancing the interaction between AtFH5 and actin filaments. Abstract : Profilin enhances the interaction between formin and actin, which assists formin with rapid actin polymerization and therefore facilitates pollen polarity formation. … (more)
- Is Part Of:
- The Plant Cell. Volume 33:Issue 4(2021)
- Journal:
- The Plant Cell
- Issue:
- Volume 33:Issue 4(2021)
- Issue Display:
- Volume 33, Issue 4 (2021)
- Year:
- 2021
- Volume:
- 33
- Issue:
- 4
- Issue Sort Value:
- 2021-0033-0004-0000
- Page Start:
- 1252
- Page End:
- 1267
- Publication Date:
- 2021-02-08
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1093/plcell/koab027 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 24966.xml