Assembly of the beta 4-Integrin Interactome Based on Proximal Biotinylation in the Presence and Absence of Heterodimerization

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Myllymaki , S-M , Kämäräinen , U-R , Liu , X , Cruz , S P , Miettinen , S , Vuorela , M , Varjosalo , M & Manninen , A 2019 , ' Assembly of the beta 4-Integrin Interactome Based on Proximal Biotinylation in the Presence and Absence of Heterodimerization ' , Molecular & Cellular Proteomics , vol. 18 , no. 2 , RA118.001095 , pp. 277-293 . https://doi.org/10.1074/mcp.RA118.001095

Title: Assembly of the beta 4-Integrin Interactome Based on Proximal Biotinylation in the Presence and Absence of Heterodimerization
Author: Myllymaki, Satu-Marja; Kämäräinen, Ulla-Reetta; Liu, Xiaonan; Cruz, Sara Pereira; Miettinen, Sini; Vuorela, Mikko; Varjosalo, Markku; Manninen, Aki
Contributor organization: Institute of Biotechnology
Doctoral Programme in Integrative Life Science
Doctoral Programme in Drug Research
Doctoral Programme in Biomedicine
University Management
Molecular Systems Biology
Date: 2019-02
Language: eng
Number of pages: 17
Belongs to series: Molecular & Cellular Proteomics
ISSN: 1535-9476
DOI: https://doi.org/10.1074/mcp.RA118.001095
URI: http://hdl.handle.net/10138/311762
Abstract: Integrin-mediated laminin adhesions mediate epithelial cell anchorage to basement membranes and are critical regulators of epithelial cell polarity. Integrins assemble large multiprotein complexes that link to the cytoskeleton and convey signals into the cells. Comprehensive proteomic analyses of actin network-linked focal adhesions (FA) have been performed, but the molecular composition of intermediate filament-linked hemidesmosomes (HD) remains incompletely characterized. Here we have used proximity-dependent biotin identification (BioID) technology to label and characterize the interactome of epithelia-specific beta 4-integrin that, as alpha 6 beta 4-heterodimer, forms the core of HDs. The analysis identified similar to 150 proteins that were specifically labeled by BirA-tagged integrin-beta 4. In addition to known HDs proteins, the interactome revealed proteins that may indirectly link integrin-beta 4 to actin-connected protein complexes, such as FAs and dystrophin/dystroglycan complexes. The specificity of the screening approach was validated by confirming the HD localization of two candidate beta 4-interacting proteins, utrophin (UTRN) and ELKS/Rab6-interacting/CAST family member 1 (ERC1). Interestingly, although establishment of functional HDs depends on the formation of alpha 6 beta 4-heterodimers, the assembly of beta 4-interactome was not strictly dependent on alpha 6-integrin expression. Our survey to the HD interactome sets a precedent for future studies and provides novel insight into the mechanisms of HD assembly and function of the beta 4-integrin.
Subject: INTEGRIN ALPHA-6-BETA-4
CYTOPLASMIC DOMAIN
PROTEINS
BETA-4
POLARITY
ADHESION
COMPLEX
CELLS
HEMIDESMOSOMES
ARCHITECTURE
1182 Biochemistry, cell and molecular biology
Peer reviewed: Yes
Rights: cc_by
Usage restriction: openAccess
Self-archived version: publishedVersion


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