Skelemin association with αiIbβ3 integrin: A structural model

Vitaliy Gorbatyuk; Khiem Nguyen; Nataly Podolnikova; Lalit Deshmukh; Xiaochen Lin; Tatiana Ugarova; Olga Vinogradova

doi:10.1021/bi500680s

Skelemin association with α_iIbβ₃ integrin: A structural model

Vitaliy Gorbatyuk, Khiem Nguyen, Nataly Podolnikova, Lalit Deshmukh, Xiaochen Lin, Tatiana Ugarova, Olga Vinogradova

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

Over the last two decades, our knowledge concerning intracellular events that regulate integrins 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_IIbβ₃. 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.

Original language	English (US)
Pages (from-to)	6766-6775
Number of pages	10
Journal	Biochemistry
Volume	53
Issue number	43
DOIs	https://doi.org/10.1021/bi500680s
State	Published - Nov 4 2014

ASJC Scopus subject areas

Biochemistry

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title = "Skelemin association with αiIbβ3 integrin: A structural model",

abstract = "Over the last two decades, our knowledge concerning intracellular events that regulate integrins 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 αIIbβ3. 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.",

author = "Vitaliy Gorbatyuk and Khiem Nguyen and Nataly Podolnikova and Lalit Deshmukh and Xiaochen Lin and Tatiana Ugarova and Olga Vinogradova",

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T1 - Skelemin association with αiIbβ3 integrin

T2 - A structural model

AU - Gorbatyuk, Vitaliy

AU - Nguyen, Khiem

AU - Podolnikova, Nataly

AU - Deshmukh, Lalit

AU - Lin, Xiaochen

AU - Ugarova, Tatiana

AU - Vinogradova, Olga

PY - 2014/11/4

Y1 - 2014/11/4

N2 - Over the last two decades, our knowledge concerning intracellular events that regulate integrins 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 αIIbβ3. 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.

AB - Over the last two decades, our knowledge concerning intracellular events that regulate integrins 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 αIIbβ3. 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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Skelemin association with α_iIbβ₃ integrin: A structural model

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