Linked Life Data

7706265

Source:http://linkedlifedata.com/resource/pubmed/id/7706265

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1995-5-10
pubmed:abstractText
In this study we have used several complementary techniques to explore the interaction between the membrane linker molecule, ankyrin, and the inositol 1,4,5-trisphosphate (IP3) receptor in mouse T-lymphoma cells. Using double immunolabeling and laser confocal microscopy, we have found that both cytoplasmic IP3 receptor and ankyrin are preferentially accumulated within ligand-induced lymphocyte receptor-capped structures. The binding between ankyrin and IP3 receptor appears to be very specific. Further analyses indicate that the amino acid sequence GGVGDVLRKPS in the IP3 receptor shares a great deal of structural homology with the ankyrin-binding domain located in certain well characterized ankyrin-binding proteins such as the cell adhesion molecule, CD44. Biochemical studies using competition binding assays and a synthetic peptide identical to GGVGDVLRKPS (a sequence detected in rat brain IP3 receptor (amino acids 2548-2558) and mouse brain IP3 receptor (amino acids 2546-2556)) indicate that this 11-amino acid peptide binds specifically to ankyrin (but not fodrin or spectrin). Furthermore, this peptide competes effectively for ankyrin binding to IP3 receptor-containing vesicles and/or purified IP3 receptor, and it blocks ankyrin-induced inhibitory effects on IP3 binding and IP3-mediated internal Ca2+ release in mouse T-lymphoma cells. These findings suggest that this amino acid sequence, GGVGDVLRKPS, which is located close to the C terminus of the IP3 receptor, resides on the cytoplasmic side (not the luminal side) of IP3 receptor-containing vesicles. This unique region appears to be an important part of the IP3 receptor ankyrin-binding domain and may play an important role in the regulation of IP3 receptor-mediated internal Ca2+ release during lymphocyte activation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7257-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7706265-Amino Acid Sequence, pubmed-meshheading:7706265-Animals, pubmed-meshheading:7706265-Ankyrins, pubmed-meshheading:7706265-Binding Sites, pubmed-meshheading:7706265-Brain, pubmed-meshheading:7706265-Calcium, pubmed-meshheading:7706265-Calcium Channels, pubmed-meshheading:7706265-Cell Line, pubmed-meshheading:7706265-Cytoskeletal Proteins, pubmed-meshheading:7706265-Fluorescent Antibody Technique, pubmed-meshheading:7706265-Inositol 1,4,5-Trisphosphate, pubmed-meshheading:7706265-Inositol 1,4,5-Trisphosphate Receptors, pubmed-meshheading:7706265-Iodine Radioisotopes, pubmed-meshheading:7706265-Kinetics, pubmed-meshheading:7706265-Lymphoma, T-Cell, pubmed-meshheading:7706265-Mice, pubmed-meshheading:7706265-Molecular Sequence Data, pubmed-meshheading:7706265-Radioligand Assay, pubmed-meshheading:7706265-Rats, pubmed-meshheading:7706265-Receptors, Cytoplasmic and Nuclear
pubmed:year
1995
pubmed:articleTitle
Identification of the ankyrin-binding domain of the mouse T-lymphoma cell inositol 1,4,5-trisphosphate (IP3) receptor and its role in the regulation of IP3-mediated internal Ca2+ release.
pubmed:affiliation
Department of Cell Biology and Anatomy, University of Miami Medical School, Florida 33101, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't