Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae

Cell. 1991 Aug 9;66(3):497-505. doi: 10.1016/0092-8674(81)90013-1.

Abstract

CAP is a component of the S. cerevisiae adenylyl cyclase complex. The N-terminal domain is required for cellular RAS responsiveness. Loss of the C-terminal domain is associated with morphological and nutritional defects. Here we report that cap- cells bud randomly and are defective in actin distribution. The morphological and nutritional defects associated with loss of the CAP C-terminal domain are suppressed by over-expression of PFY, the gene encoding profilin, an actin- and polyphosphoinositide-binding protein. The phenotype of cells lacking PFY resembles that of cells lacking the CAP C-terminal domain. Study of mutated yeast profilins and profilins from Acanthamoeba suggests that the ability of profilin to suppress cap- cells is dependent upon a property other than, or in addition to, its ability to bind actin. This property may be its ability to bind polyphosphoinositides. We propose that CAP and profilin provide a link between growth signals and remodeling of the cellular cytoskeleton.

Publication types

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

MeSH terms

  • Actins / physiology
  • Adenylyl Cyclases / physiology*
  • Amino Acid Sequence
  • Base Sequence
  • Cell Division
  • Cloning, Molecular
  • Contractile Proteins*
  • Cytoskeleton / physiology
  • DNA Mutational Analysis
  • DNA, Fungal / genetics
  • Fungal Proteins / metabolism*
  • Genes, Fungal
  • Microfilament Proteins / physiology*
  • Molecular Sequence Data
  • Oligonucleotides / chemistry
  • Profilins
  • Restriction Mapping
  • Saccharomyces cerevisiae / physiology*

Substances

  • Actins
  • Contractile Proteins
  • DNA, Fungal
  • Fungal Proteins
  • Microfilament Proteins
  • Oligonucleotides
  • Profilins
  • Adenylyl Cyclases