PIN structures shed light on their mechanism of auxin efflux
© The Author(s) 2023. Published by Oxford University Press on behalf of the Society for Experimental Biology.
| Veröffentlicht in: | Journal of experimental botany. - 1985. - 74(2023), 15 vom: 17. Aug., Seite 4377-4383 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2023
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| Zugriff auf das übergeordnete Werk: | Journal of experimental botany |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Auxin efflux hormone transport molecular mechanism polar protein structure Indoleacetic Acids Arabidopsis Proteins |
| Zusammenfassung: | © The Author(s) 2023. Published by Oxford University Press on behalf of the Society for Experimental Biology. Polar auxin transport is a quintessential feature of higher plant physiology and it has been known for many years that some of the primary drivers of polar auxin transport are the PIN-formed (PIN) auxin efflux proteins. Formative research established many key biochemical features of the transport system and discovered inhibitors such as 1-naphthylphthalamic acid (NPA), but the mechanism of action of PINs has remained elusive. This changed in 2022 with the publication of high-resolution structures of the membrane-spanning domains of three PIN proteins. The atomic structures and associated activity assays reveal that PINs use an elevator mechanism to transport auxin anions out of the cell. NPA was shown to be a competitive inhibitor that traps PINs in their inward-open conformation. The secrets of the hydrophilic cytoplasmic loop of PIN proteins remain to be discovered |
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| Beschreibung: | Date Completed 18.08.2023 Date Revised 19.08.2023 published: Print Citation Status MEDLINE |
| ISSN: | 1460-2431 |
| DOI: | 10.1093/jxb/erad185 |