Linked Life Data

14617149

Source:http://linkedlifedata.com/resource/pubmed/id/14617149

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-11-17
pubmed:abstractText
Glycosylphosphatidylinositol (GPI)-anchored cell wall proteins play an important role in the structure and function of the cell wall in yeast and other fungi. Although the majority of characterized fungal GPI-anchored proteins do in fact localize to the cell wall, some are believed to reside at the plasma membrane and not to traffic significantly to the cell wall. There is evidence suggesting that the amino acids immediately upstream of the site of GPI anchor addition (the omega site) serve as the signal determining whether a GPI protein localizes to the cell wall or to the plasma membrane, although this remains controversial. Here, we examine in detail the functional and biochemical differences between the GPI anchor addition signals of putative cell wall (CW) and plasma membrane (PM) GPI proteins. We find strong evidence for the existence of PM-class and CW-class GPI proteins. We show that the biological function of a GPI-CWP is strongly compromised by changing the GPI anchor signal from a CW-class signal to a PM-class signal. Biochemically, this abrogation of function corresponds to a change in the protein from a cell wall form to a membrane form. To understand better the basis for the difference between the two classes of proteins, we mutated the amino acids upstream of the omega site in a GPI-PM protein and selected mutant proteins that were now localized to the cell wall. We were also able to design simple amino acid mutations in a GPI-CW protein that efficiently redirected the protein to the plasma membrane. These studies make clear that different GPI anchor sequences can have dramatic effects on localization of the proteins and help to define the GPI anchor addition signal sequences that distinguish the PM-class and CW-class GPI proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
883-96
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
The omega-site sequence of glycosylphosphatidylinositol-anchored proteins in Saccharomyces cerevisiae can determine distribution between the membrane and the cell wall.
pubmed:affiliation
Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, PCTB 522, 725 N. Wolfe Street, Baltimore, MD 21205-2185, USA.
pubmed:publicationType
Journal Article