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Skelemin Association with α(IIb)β(3) Integrin: A Structural Model

[Image: see text] Over the last two decades, our knowledge concerning intracellular events that regulate integrin’s affinity to their soluble ligands has significantly improved. However, the mechanism of adhesion-induced integrin clustering and development of focal complexes, which could further mat...

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Autores principales: Gorbatyuk, Vitaliy, Nguyen, Khiem, Podolnikova, Nataly P., Deshmukh, Lalit, Lin, Xiaochen, Ugarova, Tatiana P., Vinogradova, Olga
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4222533/
https://www.ncbi.nlm.nih.gov/pubmed/25224262
http://dx.doi.org/10.1021/bi500680s
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author Gorbatyuk, Vitaliy
Nguyen, Khiem
Podolnikova, Nataly P.
Deshmukh, Lalit
Lin, Xiaochen
Ugarova, Tatiana P.
Vinogradova, Olga
author_facet Gorbatyuk, Vitaliy
Nguyen, Khiem
Podolnikova, Nataly P.
Deshmukh, Lalit
Lin, Xiaochen
Ugarova, Tatiana P.
Vinogradova, Olga
author_sort Gorbatyuk, Vitaliy
collection PubMed
description [Image: see text] Over the last two decades, our knowledge concerning intracellular events that regulate integrin’s affinity to their soluble ligands has significantly improved. However, the mechanism of adhesion-induced integrin clustering and development of focal complexes, which could further mature to form focal adhesions, still remains under-investigated. Here we present a structural model of tandem IgC2 domains of skelemin in complex with the cytoplasmic tails of integrin α(IIb)β(3). The model of tertiary assembly is generated based upon NMR data and illuminates a potential link between the essential cell adhesion receptors and myosin filaments. This connection may serve as a basis for generating the mechanical forces necessary for cell migration and remodeling.
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spelling pubmed-42225332015-09-15 Skelemin Association with α(IIb)β(3) Integrin: A Structural Model Gorbatyuk, Vitaliy Nguyen, Khiem Podolnikova, Nataly P. Deshmukh, Lalit Lin, Xiaochen Ugarova, Tatiana P. Vinogradova, Olga Biochemistry [Image: see text] Over the last two decades, our knowledge concerning intracellular events that regulate integrin’s affinity to their soluble ligands has significantly improved. However, the mechanism of adhesion-induced integrin clustering and development of focal complexes, which could further mature to form focal adhesions, still remains under-investigated. Here we present a structural model of tandem IgC2 domains of skelemin in complex with the cytoplasmic tails of integrin α(IIb)β(3). The model of tertiary assembly is generated based upon NMR data and illuminates a potential link between the essential cell adhesion receptors and myosin filaments. This connection may serve as a basis for generating the mechanical forces necessary for cell migration and remodeling. American Chemical Society 2014-09-15 2014-11-04 /pmc/articles/PMC4222533/ /pubmed/25224262 http://dx.doi.org/10.1021/bi500680s Text en Copyright © 2014 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Gorbatyuk, Vitaliy
Nguyen, Khiem
Podolnikova, Nataly P.
Deshmukh, Lalit
Lin, Xiaochen
Ugarova, Tatiana P.
Vinogradova, Olga
Skelemin Association with α(IIb)β(3) Integrin: A Structural Model
title Skelemin Association with α(IIb)β(3) Integrin: A Structural Model
title_full Skelemin Association with α(IIb)β(3) Integrin: A Structural Model
title_fullStr Skelemin Association with α(IIb)β(3) Integrin: A Structural Model
title_full_unstemmed Skelemin Association with α(IIb)β(3) Integrin: A Structural Model
title_short Skelemin Association with α(IIb)β(3) Integrin: A Structural Model
title_sort skelemin association with α(iib)β(3) integrin: a structural model
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4222533/
https://www.ncbi.nlm.nih.gov/pubmed/25224262
http://dx.doi.org/10.1021/bi500680s
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