Source:http://linkedlifedata.com/resource/pubmed/id/21454358
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2011-7-1
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| pubmed:abstractText |
T cell migration, essential for immune surveillance and response, is mediated by the integrin LFA-1. CatX, a cysteine carboxypeptidase, is involved in the regulation of T cell migration by interaction with LFA-1. We show that sequential cleavage of C-terminal amino acids from the ?(2) cytoplasmic tail of LFA-1, by CatX, enhances binding of the adaptor protein talin to LFA-1 and triggers formation of the latter's high-affinity form. As shown by SPR analysis of peptides constituting the truncated ?(2) tail, the cleavage of three C-terminal amino acids by CatX resulted in a 1.6-fold increase of talin binding. Removal of one more amino acid resulted in a 2.5-fold increase over the intact tail. CatX cleavage increased talin-binding affinity to the MD but not the MP talin-binding site on the ?(2) tail. This was shown by molecular modeling of the ?(2) tail/talin F3 complex to be a result of conformational changes affecting primarily the distal-binding site. Analysis of LFA-1 by conformation-specific mAb showed that CatX modulates LFA-1 affinity, promoting formation of high-affinity from intermediate-affinity LFA-1 but not the initial activation of LFA-1 from a bent to extended form. CatX post-translational modifications may thus represent a mechanism of LFA-1 fine-tuning that enables the trafficking of T cells.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
1938-3673
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
90
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
99-109
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| pubmed:meshHeading |
pubmed-meshheading:21454358-Antigens, CD18,
pubmed-meshheading:21454358-Blotting, Western,
pubmed-meshheading:21454358-Cathepsins,
pubmed-meshheading:21454358-Cell Separation,
pubmed-meshheading:21454358-Chemotaxis, Leukocyte,
pubmed-meshheading:21454358-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:21454358-Flow Cytometry,
pubmed-meshheading:21454358-Humans,
pubmed-meshheading:21454358-Immunoprecipitation,
pubmed-meshheading:21454358-Jurkat Cells,
pubmed-meshheading:21454358-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:21454358-Microscopy, Fluorescence,
pubmed-meshheading:21454358-Models, Molecular,
pubmed-meshheading:21454358-Polymerase Chain Reaction,
pubmed-meshheading:21454358-Protein Binding,
pubmed-meshheading:21454358-Protein Processing, Post-Translational,
pubmed-meshheading:21454358-T-Lymphocytes,
pubmed-meshheading:21454358-Talin,
pubmed-meshheading:21454358-Transfection
|
| pubmed:year |
2011
|
| pubmed:articleTitle |
Cathepsin X cleavage of the beta2 integrin regulates talin-binding and LFA-1 affinity in T cells.
|
| pubmed:affiliation |
University of Ljubljana, Askerceva 7, 1000 Ljubljana, Slovenia. zala.jevnikar@ffa.uni-lj.si
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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