Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae
dc.contributor.author | Vojtek, Anne | en_US |
dc.contributor.author | Haarer, Brian | en_US |
dc.contributor.author | Field, Jeffrey | en_US |
dc.contributor.author | Gerst, Jeffrey | en_US |
dc.contributor.author | Pollard, Thomas D. | en_US |
dc.contributor.author | Brown, Susan | en_US |
dc.contributor.author | Wigler, Michael | en_US |
dc.date.accessioned | 2006-04-10T14:37:08Z | |
dc.date.available | 2006-04-10T14:37:08Z | |
dc.date.issued | 1991-08-09 | en_US |
dc.identifier.citation | Vojtek, Anne, Haarer, Brian, Field, Jeffrey, Gerst, Jeffrey, Pollard, Thomas D., Brown, Susan, Wigler, Michael (1991/08/09)."Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae." Cell 66(3): 497-505. <http://hdl.handle.net/2027.42/29178> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WSN-4C59101-8J/2/e80cb0c16dd980e52f1dc985564e0db9 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/29178 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1868547&dopt=citation | en_US |
dc.description.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. | en_US |
dc.format.extent | 2199663 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Anatomy and Cell Biology The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Department of Anatomy and Cell Biology The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationother | Cold Spring Harbor Laboratory P.O. Box 100, Cold Spring Harbor, New York 11724-2208, USA | en_US |
dc.contributor.affiliationother | Cold Spring Harbor Laboratory P.O. Box 100, Cold Spring Harbor, New York 11724-2208, USA | en_US |
dc.contributor.affiliationother | Cold Spring Harbor Laboratory P.O. Box 100, Cold Spring Harbor, New York 11724-2208, USA | en_US |
dc.contributor.affiliationother | Department of Cell Biology and Anatomy The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA | en_US |
dc.contributor.affiliationother | Cold Spring Harbor Laboratory P.O. Box 100, Cold Spring Harbor, New York 11724-2208, USA | en_US |
dc.identifier.pmid | 1868547 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/29178/1/0000225.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0092-8674(81)90013-1 | en_US |
dc.identifier.source | Cell | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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