Linked Life Data

8663233

Source:http://linkedlifedata.com/resource/pubmed/id/8663233

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1996-8-29
pubmed:abstractText
LIM domains, Cys-rich motifs containing approximately 50 amino acids found in a variety of proteins, are proposed to direct protein*protein interactions. To identify structural targets recognized by LIM domains, we have utilized random peptide library selection, the yeast two-hybrid system, and glutathione S-transferase fusions. Enigma contains three LIM domains within its carboxyl terminus and LIM3 of Enigma specifically recognizes active but not mutant endocytic codes of the insulin receptor (InsR) (Wu, R. Y., and Gill, G. N. (1994) J. Biol. Chem. 269, 25085-25090). Interaction of two random peptide libraries with glutathione S-transferase-LIM3 of Enigma indicated specific binding to Gly-Pro-Hyd-Gly-Pro-Hyd-Tyr-Ala corresponding to the major endocytic code of InsR. Peptide competition demonstrated that both Pro and Tyr residues were required for specific interaction of InsR with Enigma. In contrast to LIM3 of Enigma binding to InsR, LIM2 of Enigma associated specifically with the receptor tyrosine kinase, Ret. Ret was specific for LIM2 of Enigma and did not bind other LIM domains tested. Mutational analysis indicated that the residues responsible for binding to Enigma were localized to the carboxyl-terminal 61 amino acids of Ret. A peptide corresponding to the carboxyl-terminal 20 amino acids of Ret dissociated Enigma and Ret complexes, while a mutant that changed Asn-Lys-Leu-Tyr in the peptide to Ala-Lys-Leu-Ala or a peptide corresponding to exon16 of InsR failed to disrupt the complexes, indicating the Asn-Lys-Leu-Tyr sequence of Ret is essential to the recognition motif for LIM2 of Enigma. We conclude that LIM domains of Enigma recognize tyrosine-containing motifs with specificity residing in both the LIM domains and in the target structures.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15934-41
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8663233-3T3 Cells, pubmed-meshheading:8663233-Amino Acid Sequence, pubmed-meshheading:8663233-Animals, pubmed-meshheading:8663233-Binding, Competitive, pubmed-meshheading:8663233-Consensus Sequence, pubmed-meshheading:8663233-Cysteine, pubmed-meshheading:8663233-Endocytosis, pubmed-meshheading:8663233-Exons, pubmed-meshheading:8663233-Glutathione Transferase, pubmed-meshheading:8663233-Mammals, pubmed-meshheading:8663233-Mice, pubmed-meshheading:8663233-Molecular Sequence Data, pubmed-meshheading:8663233-Oligopeptides, pubmed-meshheading:8663233-Receptor, Epidermal Growth Factor, pubmed-meshheading:8663233-Receptor, Insulin, pubmed-meshheading:8663233-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:8663233-Recombinant Fusion Proteins, pubmed-meshheading:8663233-Saccharomyces cerevisiae, pubmed-meshheading:8663233-Substrate Specificity, pubmed-meshheading:8663233-Transfection
pubmed:year
1996
pubmed:articleTitle
Specificity of LIM domain interactions with receptor tyrosine kinases.
pubmed:affiliation
Department of Biology, University of California San Diego, La Jolla, California 92093-0650, 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