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  New insights into the phosphorylation of the threonine motif of the β1 integrin cytoplasmic domain

Böttcher, R. T., Strohmeyer, N., Aretz, J., & Fässler, R. (2022). New insights into the phosphorylation of the threonine motif of the β1 integrin cytoplasmic domain. Life science alliance, 5(4): e202101301. doi:10.26508/lsa.202101301.

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© 2022 Böttcher et al.

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 Creators:
Böttcher, Ralph T.1, Author              
Strohmeyer, Nico2, Author
Aretz, Jonas1, Author              
Fässler, Reinhard1, Author              
Affiliations:
1Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
2external, ou_persistent22              

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Free keywords: ADHESION MEASUREMENTS; INTEGRIN ACTIVATION; CELL-ADHESION; BINDING; BETA(1)-INTEGRIN; FILAMIN; IDENTIFICATION; TYROSINES; PROTEINS; AFFINITYLife Sciences & Biomedicine - Other Topics;
 Abstract: Integrins require an activation step before ligand binding and signaling that is mediated by talin and kindlin binding to the beta integrin cytosolic domain (beta-tail). Conflicting reports exist about the contribution of phosphorylation of a conserved threonine motif in the beta 1-tail (beta 1-pT788/pT789) to integrin activation. We show that widely used and commercially available antibodies against beta 1-pT788/pT789 integrin do not detect specific beta 1-pT788/ pT789 integrin signals in immunoblots of several human and mouse cell lysates but bind bi-phosphorylated threonine resi-dues in numerous proteins, which were identified by mass spectrometry experiments. Furthermore, we found that fibro-blasts and epithelial cells expressing the phospho-mimicking beta 1-TT788/789DD integrin failed to activate beta 1 integrins and displayed reduced integrin ligand binding, adhesion initiation and cell spreading. These cellular defects are specifically caused by the inability of kindlin to bind beta 1-tail polypeptides carrying a phosphorylated threonine motif or phospho-mimicking TT788/789DD substitutions. Our findings indicate that the double-threonine motif in beta 1-class integrins is not a major phosphory-lation site but if phosphorylated would curb integrin function.

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Language(s): eng - English
 Dates: 2022-012022-04
 Publication Status: Published in print
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000742638600002
DOI: 10.26508/lsa.202101301
 Degree: -

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Project name : SFB914
Grant ID : -
Funding program : -
Funding organization : Deutsche Forschungsgemeinschaft
Project name : -
Grant ID : 810104
Funding program : -
Funding organization : European Research Council

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Title: Life science alliance
  Abbreviation : Life Sci Alliance
Source Genre: Journal
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Publ. Info: Heidelberg : EMBO Press
Pages: - Volume / Issue: 5 (4) Sequence Number: e202101301 Start / End Page: - Identifier: ISSN: 2575-1077
CoNE: https://pure.mpg.de/cone/journals/resource/2575-1077