Subcellular localization of Axl1, the cell type-specific regulator of polarity

Curr Biol. 2002 Aug 6;12(15):1347-52. doi: 10.1016/s0960-9822(02)01042-4.


Bud-site selection in yeast offers an attractive system for studying cell polarity and asymmetric division. Haploids divide in an axial pattern, whereas diploids divide in a bipolar pattern. AXL1 is expressed in haploids but not diploids, and ectopic expression of AXL1 in diploids converts their bipolar budding pattern to an axial pattern. How Axl1 acts as a switch between the bipolar and axial patterns is not understood. Here we report that Axl1 localizes to the mother-bud neck and division site remnants of haploids. Axl1 is absent from diploids. Axl1 colocalizes with Bud3, Bud4, and Bud10, components of the axial landmark structure. This localization suggests that Axl1 couples the axial landmark with downstream polarity establishment factors. Consistent with such a role, Axl1 associated biochemically with Bud4 and Bud5. Genetic evidence suggests that Axl1 works with Bud3 and Bud4 to promote the activity of the Bud10 membrane protein. Given Axl1's suggested role in morphogenesis and cell fusion during mating, we also examined its localization during this process. Axl1 redistributes independently of the axial landmark to a tight cell surface dot at the tip of each mating projection. These dots are rapidly lost as prezygotes form.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cell Division
  • Cell Polarity / physiology*
  • Diploidy
  • Gene Expression Regulation, Fungal
  • Genotype
  • Haploidy
  • Insulysin / metabolism
  • Metalloendopeptidases
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*


  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • AXL1 protein, S cerevisiae
  • Metalloendopeptidases
  • Insulysin