Linked Life Data

7673216

Source:http://linkedlifedata.com/resource/pubmed/id/7673216

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
38
pubmed:dateCreated
1995-10-17
pubmed:databankReference
pubmed:abstractText
The Saccharomyces cerevisiae vacuolar H(+)-ATPase (V-ATPase) is a multi-subunit complex that can be structurally and functionally divided into peripheral (V1) and integral membrane (V0) sectors. The vma22-1 mutation was isolated in a screen for mutants defective in V-ATPase function vma22 delta cells contain no V-ATPase activity due to a failure to assemble the enzyme complex; V1 subunits accumulate in the cytosol, and the V0 100-kDa subunit is rapidly degraded. Turnover of the 100-kDa integral membrane protein was found to occur in the endoplasmic reticulum (ER) of vma22 delta cells. The product of the VMA22 gene, Vma22p, is a 21-kDa hydrophilic protein that is not a subunit of the V-ATPase but rather is associated with ER membranes. The association of Vma22p with ER membranes was perturbed by mutations in VMA12, a gene that encodes an ER membrane protein (Vma12p) that is also required for V-ATPase assembly. These results indicate that Vma22p, along with Vma21p and Vma12p, form a set of ER proteins required for V-ATPase assembly.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22329-36
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H(+)-ATPase complex.
pubmed:affiliation
Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't