The Role of LORELEI in Pollen Tube Reception at the Interface of the Synergid Cell and Pollen Tube Requires the Modified Eight-Cysteine Motif and the Receptor-Like Kinase FERONIA. Issue 5 (14th April 2016)
- Record Type:
- Journal Article
- Title:
- The Role of LORELEI in Pollen Tube Reception at the Interface of the Synergid Cell and Pollen Tube Requires the Modified Eight-Cysteine Motif and the Receptor-Like Kinase FERONIA. Issue 5 (14th April 2016)
- Main Title:
- The Role of LORELEI in Pollen Tube Reception at the Interface of the Synergid Cell and Pollen Tube Requires the Modified Eight-Cysteine Motif and the Receptor-Like Kinase FERONIA
- Authors:
- Liu, Xunliang
Castro, Claudia
Wang, Yanbing
Noble, Jennifer
Ponvert, Nathaniel
Bundy, Mark
Hoel, Chelsea
Shpak, Elena
Palanivelu, Ravishankar - Abstract:
- Abstract : Structure-function analysis reveals domains in LORELEI critical for its role in pollen tube reception at the synergid surface, which it performs in conjunction with the receptor-like kinase FERONIA. Abstract: In angiosperms, pollen tube reception by the female gametophyte is required for sperm release and double fertilization. In Arabidopsis thaliana lorelei ( lre ) mutants, pollen tube reception fails in most female gametophytes, which thus remain unfertilized. LRE encodes a putative glycosylphosphatidylinositol (GPI )-anchored surface protein with a modified eight-cysteine motif (M8CM ). LRE fused to citrine yellow fluorescent protein (LRE-cYFP) remains functional and localizes to the synergid plasma membrane-rich filiform apparatus, the first point of contact between the pollen tube and the female gametophyte. Structure-function analysis using LRE-cYFP showed that the role of LRE in pollen tube reception requires the M8CM, but not the domains required for GPI anchor addition. Consistently, LRE-cYFP-TM, where GPI anchor addition domains were replaced with a single-pass transmembrane domain, fully complemented the pollen tube reception defect in lre-7 female gametophytes. Ectopically expressed and delivered LRE-cYFP from pollen tubes could non-cell-autonomously complement the pollen tube reception defect in lre female gametophytes, only if they expressed FERONIA. Additionally, pollen tube-expressing LRE variants lacking domains critical for GPI anchor additionAbstract : Structure-function analysis reveals domains in LORELEI critical for its role in pollen tube reception at the synergid surface, which it performs in conjunction with the receptor-like kinase FERONIA. Abstract: In angiosperms, pollen tube reception by the female gametophyte is required for sperm release and double fertilization. In Arabidopsis thaliana lorelei ( lre ) mutants, pollen tube reception fails in most female gametophytes, which thus remain unfertilized. LRE encodes a putative glycosylphosphatidylinositol (GPI )-anchored surface protein with a modified eight-cysteine motif (M8CM ). LRE fused to citrine yellow fluorescent protein (LRE-cYFP) remains functional and localizes to the synergid plasma membrane-rich filiform apparatus, the first point of contact between the pollen tube and the female gametophyte. Structure-function analysis using LRE-cYFP showed that the role of LRE in pollen tube reception requires the M8CM, but not the domains required for GPI anchor addition. Consistently, LRE-cYFP-TM, where GPI anchor addition domains were replaced with a single-pass transmembrane domain, fully complemented the pollen tube reception defect in lre-7 female gametophytes. Ectopically expressed and delivered LRE-cYFP from pollen tubes could non-cell-autonomously complement the pollen tube reception defect in lre female gametophytes, only if they expressed FERONIA. Additionally, pollen tube-expressing LRE variants lacking domains critical for GPI anchor addition also rescued lre female gametophyte function. Therefore, LRE and FERONIA jointly function in pollen tube reception at the interface of the synergid cell and pollen tube. … (more)
- Is Part Of:
- The Plant Cell. Volume 28:Issue 5(2016)
- Journal:
- The Plant Cell
- Issue:
- Volume 28:Issue 5(2016)
- Issue Display:
- Volume 28, Issue 5 (2016)
- Year:
- 2016
- Volume:
- 28
- Issue:
- 5
- Issue Sort Value:
- 2016-0028-0005-0000
- Page Start:
- 1035
- Page End:
- 1052
- Publication Date:
- 2016-04-14
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.15.00703 ↗
- 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:
- 16319.xml