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

• Published in: Cell Vol. 66; no. 3; pp. 497 - 505
• Main Authors: Vojtek, Anne, Haarer, Brian, Field, Jeffrey, Gerst, Jeffrey, Pollard, Thomas D., Brown, Susan, Wigler, Michael
• Format: Journal Article
• Language: English
• Published: Cambridge, MA Elsevier Inc 09.08.1991; Cell Press
• Subjects: Actins - physiology; Adenylyl Cyclases - physiology; Amino Acid Sequence; Base Sequence; Biological and medical sciences; Cell Division; Cloning, Molecular; Contractile Proteins; Cytoskeleton - physiology; DNA Mutational Analysis; DNA, Fungal - genetics; Fundamental and applied biological sciences. Psychology; Fungal Proteins - metabolism; Genes, Fungal; Microfilament Proteins - physiology; Miscellaneous; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Oligonucleotides - chemistry; Profilins; Restriction Mapping; Saccharomyces cerevisiae - physiology; Phosphoinositide; Yeast; C terminal peptide; Enzyme; Gene product; Actins; Molecular interaction; Metabolism; Fungi; Adenylate cyclase; Morphology; Point mutation; Cytoskeleton; Ascomycetes; Saccharomyces cerevisiae; Thallophyta; G protein
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/0092-8674(81)90013-1

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.