ArticlePlant physiology2016
Sorting Motifs Involved in the Trafficking and Localization of the PIN1 Auxin Efflux Carrier.
Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- ROPGAP3 interacts with PIN2 and modulates its clustering and trafficking inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants.The Plant cell · 2024Review
- Genome Identification and Expression Profiling of theInternational journal of molecular sciences · 2024Article
- Regulation of PIN-FORMED Protein Degradation.International journal of molecular sciences · 2023Review
- The Hydrophilic Loop ofInternational journal of molecular sciences · 2022Article
- Auxin Transporters-A Biochemical View.Cold Spring Harbor perspectives in biology · 2022Review
- Molecular mechanisms of endomembrane trafficking in plants.The Plant cell · 2022Review
- Expression analysis ofFrontiers in plant science · 2022Article
- Systematic analysis of specific and nonspecific auxin effects on endocytosis and trafficking.Plant physiology · 2021Article
- Motif-based endomembrane trafficking.Plant physiology · 2021Article
- Endocytosis of BRASSINOSTEROID INSENSITIVE1 Is Partly Driven by a Canonical Tyr-Based Motif.The Plant cell · 2020Article
- Strigolactones inhibit auxin feedback on PIN-dependent auxin transport canalization.Nature communications · 2020Article
- Root Growth Adaptation is Mediated by PYLs ABA Receptor-PP2A Protein Phosphatase Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- The Beginning of the End: Initial Steps in the Degradation of Plasma Membrane Proteins.Frontiers in plant science · 2020Review
- Remove, Recycle, Degrade: Regulating Plasma Membrane Protein Accumulation.The Plant cell · 2019Review
- Comparative Analysis of the PIN Auxin Transporter Gene Family in Different Plant Species: A Focus on Structural and Expression Profiling of PINs inInternational journal of molecular sciences · 2019Article
- Polar Localization of the Borate Exporter BOR1 Requires AP2-Dependent Endocytosis.Plant physiology · 2019Article
- The Nuts and Bolts of PIN Auxin Efflux Carriers.Frontiers in plant science · 2019Review
- Inroads into Internalization: Five Years of Endocytic Exploration.Plant physiology · 2018Review
- α2-COP is involved in early secretory traffic in Arabidopsis and is required for plant growth.Journal of experimental botany · 2017Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In contrast with the wealth of recent reports about the function of μ-adaptins and clathrin adaptor protein (AP) complexes, there is very little information about the motifs that determine the sorting of membrane proteins within clathrin-coated vesicles in plants. Here, we investigated putative sorting signals in the large cytosolic loop of the Arabidopsis (Arabidopsis thaliana) PIN-FORMED1 (PIN1) auxin transporter, which are involved in binding μ-adaptins and thus in PIN1 trafficking and localization. We found that Phe-165 and Tyr-280, Tyr-328, and Tyr-394 are involved in the binding of different μ-adaptins in vitro. However, only Phe-165, which binds μA(μ2)- and μD(μ3)-adaptin, was found to be essential for PIN1 trafficking and localization in vivo. The PIN1:GFP-F165A mutant showed reduced endocytosis but also localized to intracellular structures containing several layers of membranes and endoplasmic reticulum (ER) markers, suggesting that they correspond to ER or ER-derived membranes. While PIN1:GFP localized normally in a μA (μ2)-adaptin mutant, it accumulated in big intracellular structures containing LysoTracker in a μD (μ3)-adaptin mutant, consistent with previous results obtained with mutants of other subunits of the AP-3 complex. Our data suggest that Phe-165, through the binding of μA (μ2)- and μD (μ3)-adaptin, is important for PIN1 endocytosis and for PIN1 trafficking along the secretory pathway, respectively.
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Registered trials
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