ArticlePLoS genetics2017
BAK1 is involved in AtRALF1-induced inhibition of root cell expansion.
Article in PLoS genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 57 citations in OpenAlex.
- Epigenetic regulation of TaFIP phytocytokine clusters confers basal resistance via receptor kinase TaFIPR in wheat.Nature plants · 2026Article
- OsRALF26 Serves as an Endogenous Signal Recognised by XA21 to Promote Robust and Distal Resistance in Rice.Plant biotechnology journal · 2026Article
- The RALF-FERONIA Signaling Axis: A Central Hub Integrating Plant Growth, Reproduction, and Stress Responses.International journal of molecular sciences · 2025Review
- Peptides and Reactive Oxygen Species Regulate Root Development.International journal of molecular sciences · 2025Review
- LRR-RLK subfamily II of coreceptors: emerging, non-canonical and canonical roles in plant antiviral immunity and development.Frontiers in plant science · 2025Review
- Genome-Wide Identification of thePlants (Basel, Switzerland) · 2024Article
- Bioinformatic and Phenotypic Analysis ofPlants (Basel, Switzerland) · 2024Article
- FERONIA: A Receptor Kinase at the Core of a Global Signaling Network.Annual review of plant biology · 2024Review
- The plant cell wall-dynamic, strong, and adaptable-is a natural shapeshifter.The Plant cell · 2024Review
- Rapid alkalinization factor: function, regulation, and potential applications in agriculture.Stress biology · 2023Review
- RALF1 peptide triggers biphasic root growth inhibition upstream of auxin biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Genome-Wide Identification of Rapid Alkalinization Factor Family inFrontiers in plant science · 2022Article
- Malectin/Malectin-like domain-containing proteins: A repertoire of cell surface molecules with broad functional potential.Cell surface (Amsterdam, Netherlands) · 2021Review
- CALMODULIN-LIKE-38 and PEP1 RECEPTOR 2 integrate nitrate and brassinosteroid signals to regulate root growth.Plant physiology · 2021Article
- Family-wide evaluation of RAPID ALKALINIZATION FACTOR peptides.Plant physiology · 2021Article
- PbrRALF2-elicited reactive oxygen species signaling is mediated by the PbrCrRLK1L13-PbrMPK18 module in pear pollen tubes.Horticulture research · 2021Article
- Article
- The root growth reduction in response to mechanical stress involves ethylene-mediated microtubule reorganization and transmembrane receptor-mediated signal transduction in Arabidopsis.Plant cell reports · 2021Article
- Overlapping functions and protein-protein interactions of LRR-extensins in Arabidopsis.PLoS genetics · 2020Article
- Prospects of Gene Knockouts in the Functional Study of MAMP-Triggered Immunity: A Review.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rapid alkalinization factor (RALF) peptide negatively regulates cell expansion, and an antagonistic relationship has been demonstrated between AtRALF1, a root-specific RALF isoform in Arabidopsis, and brassinosteroids (BRs). An evaluation of the response of BR signaling mutants to AtRALF1 revealed that BRI1-associated receptor kinase1 (bak1) mutants are insensitive to AtRALF1 root growth inhibition activity. BAK1 was essential for the induction of AtRALF1-responsive genes but showed no effect on the mobilization of Ca2+ and alkalinization responses. Homozygous plants accumulating AtRALF1 and lacking the BAK1 gene did not exhibit the characteristic semi-dwarf phenotype of AtRALF1-overexpressors. Biochemical evidence indicates that AtRALF1 and BAK1 physically interact with a Kd of 4.6 μM and acridinium-labeled AtRALF1 was used to demonstrate that part of the specific binding of AtRALF1 to intact seedlings and to a microsomal fraction derived from the roots of Arabidopsis plants is BAK1-dependent. Moreover, AtRALF1 induces an increase in BAK1 phosphorylation, suggesting that the binding of AtRALF1 to BAK1 is functional. These findings show that BAK1 contains an additional AtRALF1 binding site, indicating that this protein may be part of a AtRALF1-containing complex as a co-receptor, and it is required for the negative regulation of cell expansion.
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