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

Persistent Link:
http://hdl.handle.net/10150/617178
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
Author:
Liu, Xunliang ( 0000-0003-0445-0343 ) ; Castro, Claudia ( 0000-0002-5164-1356 ) ; Wang, Yanbing ( 0000-0002-9064-8104 ) ; Noble, Jennifer ( 0000-0003-1019-2416 ) ; Ponvert, Nathaniel ( 0000-0003-3922-2228 ) ; Bundy, Mark ( 0000-0002-4463-3382 ) ; Hoel, Chelsea; Shpak, Elena; Palanivelu, Ravishankar ( 0000-0003-0564-5564 )
Affiliation:
Univ Arizona, Sch Plant Sci
Issue Date:
2016-05
Publisher:
AMER SOC PLANT BIOLOGISTS
Citation:
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 2016, 28 (5):1035 The Plant Cell
Journal:
The Plant Cell
Rights:
© 2016 American Society of Plant Biologists. All rights reserved.
Collection Information:
This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
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.
Note:
12 month embargo.
ISSN:
1040-4651; 1532-298X
DOI:
10.1105/tpc.15.00703
Version:
Final accepted manuscript
Sponsors:
National Science Foundation [DGE-1143953, IOS-1146090]
Additional Links:
http://www.plantcell.org/lookup/doi/10.1105/tpc.15.00703

Full metadata record

DC FieldValue Language
dc.contributor.authorLiu, Xunliangen
dc.contributor.authorCastro, Claudiaen
dc.contributor.authorWang, Yanbingen
dc.contributor.authorNoble, Jenniferen
dc.contributor.authorPonvert, Nathanielen
dc.contributor.authorBundy, Marken
dc.contributor.authorHoel, Chelseaen
dc.contributor.authorShpak, Elenaen
dc.contributor.authorPalanivelu, Ravishankaren
dc.date.accessioned2016-07-18T21:42:05Z-
dc.date.available2016-07-18T21:42:05Z-
dc.date.issued2016-05-
dc.identifier.citationThe 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 2016, 28 (5):1035 The Plant Cellen
dc.identifier.issn1040-4651-
dc.identifier.issn1532-298X-
dc.identifier.doi10.1105/tpc.15.00703-
dc.identifier.urihttp://hdl.handle.net/10150/617178-
dc.description.abstractIn 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.en
dc.description.sponsorshipNational Science Foundation [DGE-1143953, IOS-1146090]en
dc.language.isoenen
dc.publisherAMER SOC PLANT BIOLOGISTSen
dc.relation.urlhttp://www.plantcell.org/lookup/doi/10.1105/tpc.15.00703en
dc.rights© 2016 American Society of Plant Biologists. All rights reserved.en
dc.titleThe 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 FERONIAen
dc.typeArticleen
dc.contributor.departmentUniv Arizona, Sch Plant Scien
dc.identifier.journalThe Plant Cellen
dc.description.note12 month embargo.en
dc.description.collectioninformationThis item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.en
dc.eprint.versionFinal accepted manuscripten
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