Linked Life Data

9677411

Source:http://linkedlifedata.com/resource/pubmed/id/9677411

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1998-9-10
pubmed:abstractText
Arf proteins are ubiquitous, eukaryotic regulators of virtually every step of vesicular membrane traffic. ADP-ribosylation factors are essential in yeast and the lethality resulting from either overexpression or underexpression (deletion) of Arf genes has previously been ascribed to dysregulation of the secretory process. We have identified a family of four genes (Suppressors of Arf ts, SAT) as high copy suppressors of a loss of function allele of ARF1 (arf1-3). Those proteins with SAT activity were found to contain a minimal consensus motif, including a C2C2H2 cluster with a novel and specific spacing. Genetic interactions between members of this family and with ARF1 are consistent with each sharing a common cellular pathway. Included in this family is Gcs1, a protein previously described (Poon, P. P., Wang, X., Rotman, M., Huber, I., Cukierman, E., Cassel, D., Singer, R. A., and Johnston, G. C. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 10074-10077) to possess Arf GTPase-activating protein (GAP) activity, demonstrating a direct interaction between Arf and at least one of these suppressors. The suppression of the loss of Arf function by overexpression of Gcs1 and demonstration of direct, preferential binding of Gcs1 to the activated form of Arf (Arf.GTP) lead us to conclude that the biological role of Gcs1 is as an effector of the essential function of Arf in mitotic growth, rather than a down-regulator as implied by the biochemical (Arf GAP) activity. Suppression of the growth defect of arf1(-3) cells was observed under conditions that did not alter the secretory defect associated with arf1(-) mutation, indicating that the essential role of Arf in eukaryotes can be distinguished from role(s) in the secretory pathway and appear to employ distinct pathways and effectors.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19792-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9677411-ADP-Ribosylation Factor 1, pubmed-meshheading:9677411-ADP-Ribosylation Factors, pubmed-meshheading:9677411-Cell Division, pubmed-meshheading:9677411-Cloning, Molecular, pubmed-meshheading:9677411-DNA-Binding Proteins, pubmed-meshheading:9677411-Fungal Proteins, pubmed-meshheading:9677411-GTP-Binding Proteins, pubmed-meshheading:9677411-GTPase-Activating Proteins, pubmed-meshheading:9677411-Gene Expression Regulation, Fungal, pubmed-meshheading:9677411-Genes, Fungal, pubmed-meshheading:9677411-Glycoside Hydrolases, pubmed-meshheading:9677411-Mutation, pubmed-meshheading:9677411-Saccharomyces cerevisiae, pubmed-meshheading:9677411-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9677411-Sequence Alignment, pubmed-meshheading:9677411-Suppression, Genetic, pubmed-meshheading:9677411-Zinc Fingers, pubmed-meshheading:9677411-beta-Fructofuranosidase
pubmed:year
1998
pubmed:articleTitle
A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae.
pubmed:affiliation
Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322-3050, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.