Cloning of the 16-kDa V-ATPase proteolipid subunit from the red imported fire ant Solenopsis invicta buren (Hymenoptera: Formicidae). Academic Article uri icon


  • V-ATPases are ubiquitous proton pumps found in eukaryotes, and are important in regulating the pH of cell compartments and in creating membrane potentials. The V-ATPase creates a proton gradient that is used as an energy source for the transport of other ions. The 16-kDa proteolipid is the proton-translocating subunit c of V-ATPases. Using PCR methods, we have cloned the fire ant 16-kDa subunit c, providing the first molecular characterization of this protein in a social insect. Northern blot analysis revealed three possible different transcripts. The presence of V-ATPases in ant Malpighian tubules had been previously demonstrated, where they provide the proton gradient necessary for the excretion of other ions and the formation of primary urine. The 16-kDa proteolipid is highly conserved among insects, and in ants may be important to the critical processes of diuresis and olfaction as a key component of the V-ATPase. Arch.

published proceedings

  • Arch Insect Biochem Physiol

author list (cited authors)

  • Holmes, S. P., Frazier, S. K., & Pietrantonio, P. V.

citation count

  • 2

complete list of authors

  • Holmes, SP||Frazier, SK||Pietrantonio, PV

publication date

  • November 2000