Linked Life Data

9694734

Source:http://linkedlifedata.com/resource/pubmed/id/9694734

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-9-10
pubmed:abstractText
Erythrocyte protein 4.1 (P4.1) is an 80-kD cytoskeletal protein that is important for the maintenance of the structural integrity and flexibility of the red blood cell membrane. Limited chymotryptic digestion of erythroid P4.1 yields 4 structural domains corresponding to the 30-, 16-, 10-, and 22/24-kD domains. Using a yeast two-hybrid system, we isolated cDNA clones encoding pICln that specifically interacts with the 30-kD domain of P4.1. In this report, we show that the carboxyl-terminus (amino acid residues 103-237) of pICln binds to the 30-kD domain of P4.1 in a yeast two-hybrid system. The direct association between the 30-kD domain of P4.1 and pICln was further confirmed by the following findings: (1) the S35-methione-labeled pICln specifically bound to both GST/P4.1-80 (80 kD) and GST/P4.1-30 (30 kD) fusion proteins, but not to the proteins that lack the 30-kD domain; (2) coimmunoprecipitation analysis of the cell extracts from transfected SiHa cells showed that pICln and P4.1 associate in transfected cells. It was reported that pICln can form a complex with actin and may play a role involved in cellular volume regulation. The direct association between P4.1 and pICln suggests that pICln may link P4.1-bound cytoskeletal elements to an unidentified volume-sensitive chloride channel.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-4971
pubmed:author
pubmed:copyrightInfo
Copyright 1998 by The American Society of Hematology.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1442-7
pubmed:dateRevised
2011-6-20
pubmed:meshHeading
pubmed-meshheading:9694734-Cell Size, pubmed-meshheading:9694734-Chloride Channels, pubmed-meshheading:9694734-Chlorides, pubmed-meshheading:9694734-Cytoskeletal Proteins, pubmed-meshheading:9694734-Cytoskeleton, pubmed-meshheading:9694734-Erythrocytes, pubmed-meshheading:9694734-Humans, pubmed-meshheading:9694734-Ion Channels, pubmed-meshheading:9694734-Ion Transport, pubmed-meshheading:9694734-Membrane Proteins, pubmed-meshheading:9694734-Multigene Family, pubmed-meshheading:9694734-Neuropeptides, pubmed-meshheading:9694734-Protein Binding, pubmed-meshheading:9694734-Protein Structure, Tertiary, pubmed-meshheading:9694734-Recombinant Fusion Proteins, pubmed-meshheading:9694734-Saccharomyces cerevisiae, pubmed-meshheading:9694734-Sequence Deletion, pubmed-meshheading:9694734-Structure-Activity Relationship, pubmed-meshheading:9694734-Transfection
pubmed:year
1998
pubmed:articleTitle
The 30-kD domain of protein 4.1 mediates its binding to the carboxyl terminus of pICln, a protein involved in cellular volume regulation.
pubmed:affiliation
Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, Republic of China.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't