Linked Life Data

8702846

Source:http://linkedlifedata.com/resource/pubmed/id/8702846

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
1996-10-11
pubmed:databankReference
pubmed:abstractText
Assembly of alpha- and beta-subunits in the endoplasmic reticulum is a prerequisite for the structural and functional maturation of oligomeric P-type ATPases. In Xenopus oocytes, overexpressed, unassembled alpha- and beta-subunits of Xenopus Na,K-ATPase are retained in the endoplasmic reticulum (ER) and are degraded with different kinetics, while unassembled beta-subunits of gastric H, K-ATPase leave the ER. In this study, we have investigated the role of the immunoglobulin-binding protein, BiP, in the folding, assembly, and ER retention of ATPase subunits. We determined the primary sequence of Xenopus BiP and used polyclonal antibodies to examine the interaction with BiP of various wild type and mutant alpha- and beta-subunits overexpressed in Xenopus oocytes. Our results show that ER-retained, unassembled Na,K-ATPase beta-subunits, but not transport-competent H,K-ATPase beta-subunits, efficiently associate with BiP until assembly with alpha-subunits occurs. Furthermore, the kinetics of BiP interaction with unassembled wild type and with mutant Na,K-ATPase beta-subunits parallels their respective stability against cellular degradation. Finally, alpha-subunits that are overexpressed in oocytes and are rapidly degraded and endogenous oocyte alpha-subunits that are stably expressed as individual assembly-competent proteins also interact with oocyte or exogenous BiP, and the interaction time correlates with the protein's stability. These data demonstrate for the first time that BiP might be involved in a long term maturation arrest and/or in the ER quality control of a multimembrane-spanning protein and lend support for a universal chaperone function of BiP.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20895-902
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:8702846-Animals, pubmed-meshheading:8702846-Base Sequence, pubmed-meshheading:8702846-Biological Transport, pubmed-meshheading:8702846-Carrier Proteins, pubmed-meshheading:8702846-Cell Compartmentation, pubmed-meshheading:8702846-Cloning, Molecular, pubmed-meshheading:8702846-DNA, Complementary, pubmed-meshheading:8702846-DNA Primers, pubmed-meshheading:8702846-Endoplasmic Reticulum, Rough, pubmed-meshheading:8702846-H(+)-K(+)-Exchanging ATPase, pubmed-meshheading:8702846-Heat-Shock Proteins, pubmed-meshheading:8702846-Macromolecular Substances, pubmed-meshheading:8702846-Molecular Chaperones, pubmed-meshheading:8702846-Molecular Sequence Data, pubmed-meshheading:8702846-Oocytes, pubmed-meshheading:8702846-Precipitin Tests, pubmed-meshheading:8702846-Protein Binding, pubmed-meshheading:8702846-Protein Folding, pubmed-meshheading:8702846-Rats, pubmed-meshheading:8702846-Sequence Alignment, pubmed-meshheading:8702846-Sequence Homology, Amino Acid, pubmed-meshheading:8702846-Sodium-Potassium-Exchanging ATPase, pubmed-meshheading:8702846-Xenopus laevis
pubmed:year
1996
pubmed:articleTitle
Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP.
pubmed:affiliation
Institute of Pharmacology et Toxicology, University of Lausanne, rue du Bugnon 27, CH-1005 Lausanne, Switzerland.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't