ArticleThe Plant journal : for cell and molecular biology2017
Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain.
Article in The Plant journal : for cell and molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 66 citations in OpenAlex.
- A FnWRKY17-Frontiers in plant science · 2026Article
- Moisture-responsive root-branching pathways identified in diverse maize breeding germplasm.Science (New York, N.Y.) · 2025Article
- JAGGER localization and function are dependent on GPI anchor addition.Plant reproduction · 2024Article
- Distinct functions of FASCILIN-LIKE ARABINOGALACTAN PROTEINS relate to domain structure.Plant physiology · 2023Article
- Promoter and domain structures regulate FLA12 function during Arabidopsis secondary wall development.Frontiers in plant science · 2023Article
- Arabinogalactan Proteins: Focus on the Role in Cellulose Synthesis and Deposition during Plant Cell Wall Biogenesis.International journal of molecular sciences · 2022Review
- CAGEs are Golgi-localized GT31 enzymes involved in cellulose biosynthesis in Arabidopsis.The Plant journal : for cell and molecular biology · 2022Article
- Differential Expression of Arabinogalactan in Response to Inclination in Stem ofPlants (Basel, Switzerland) · 2022Article
- FLA11 and FLA12 glycoproteins fine-tune stem secondary wall properties in response to mechanical stresses.The New phytologist · 2022Article
- The regulation of the cell wall by glycosylphosphatidylinositol-anchored proteins inFrontiers in cell and developmental biology · 2022Review
- FLA14 is required for pollen development and preventing premature pollen germination under high humidity in Arabidopsis.BMC plant biology · 2021Article
- Review
- Cracking the "Sugar Code": A Snapshot ofFrontiers in plant science · 2021Review
- FASCICLIN-LIKE 18 Is a New Player Regulating Root Elongation inFrontiers in plant science · 2021Article
- Arabinogalactan Proteins in Plant Roots - An Update on Possible Functions.Frontiers in plant science · 2021Review
- Golgi-localized exo-β1,3-galactosidases involved in cell expansion and root growth inThe Journal of biological chemistry · 2020Article
- Fasciclin-like arabinogalactan gene family in Nicotiana benthamiana: genome-wide identification, classification and expression in response to pathogens.BMC plant biology · 2020Article
- Genome-wide analyses of banana fasciclin-like AGP genes and their differential expression under low-temperature stress in chilling sensitive and tolerant cultivars.Plant cell reports · 2020Article
- On the Potential Function of Type II ArabinogalactanFrontiers in plant science · 2020Review
- Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development inFrontiers in plant science · 2020Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Fasciclin-like arabinogalactan proteins (FLAs) are involved in numerous important functions in plants but the relevance of their complex structure to physiological function and cellular fate is unresolved. Using a fully functional fluorescent version of Arabidopsis thaliana FLA4 we show that this protein is localized at the plasma membrane as well as in endosomes and soluble in the apoplast. FLA4 is likely to be GPI-anchored, is highly N-glycosylated and carries two O-glycan epitopes previously associated with arabinogalactan proteins. The activity of FLA4 was resistant against deletion of the amino-proximal fasciclin 1 domain and was unaffected by removal of the GPI-modification signal, a highly conserved N-glycan or the deletion of predicted O-glycosylation sites. Nonetheless these structural changes dramatically decreased endoplasmic reticulum (ER)-exit and plasma membrane localization of FLA4, with N-glycosylation acting at the level of ER-exit and O-glycosylation influencing post-secretory fate. We show that FLA4 acts predominantly by molecular interactions involving its carboxy-proximal fasciclin 1 domain and that its amino-proximal fasciclin 1 domain is required for stabilization of plasma membrane localization. FLA4 functions as a soluble glycoprotein via its carboxy-proximal Fas1 domain and its normal cellular trafficking depends on N- and O-glycosylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.