A novel putative auxin carrier family regulates intracellular auxin homeostasis in plants

Nature. 2012 Apr 15;485(7396):119-22. doi: 10.1038/nature11001.


The phytohormone auxin acts as a prominent signal, providing, by its local accumulation or depletion in selected cells, a spatial and temporal reference for changes in the developmental program. The distribution of auxin depends on both auxin metabolism (biosynthesis, conjugation and degradation) and cellular auxin transport. We identified in silico a novel putative auxin transport facilitator family, called PIN-LIKES (PILS). Here we illustrate that PILS proteins are required for auxin-dependent regulation of plant growth by determining the cellular sensitivity to auxin. PILS proteins regulate intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signalling. PILS activity affects the level of endogenous auxin indole-3-acetic acid (IAA), presumably via intracellular accumulation and metabolism. Our findings reveal that the transport machinery to compartmentalize auxin within the cell is of an unexpected molecular complexity and demonstrate this compartmentalization to be functionally important for a number of developmental processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / cytology
  • Arabidopsis / genetics
  • Arabidopsis / growth & development
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Endoplasmic Reticulum / metabolism
  • Genes, Plant / genetics
  • Germination
  • Homeostasis*
  • Indoleacetic Acids / metabolism*
  • Intracellular Space / metabolism*
  • Multigene Family*
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism
  • Plants, Genetically Modified
  • Promoter Regions, Genetic / genetics
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism


  • Arabidopsis Proteins
  • Carrier Proteins
  • Indoleacetic Acids
  • Mutant Proteins
  • indoleacetic acid