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

Show simple item record Myllymaki, Satu-Marja Kämäräinen, Ulla-Reetta Liu, Xiaonan Cruz, Sara Pereira Miettinen, Sini Vuorela, Mikko Varjosalo, Markku Manninen, Aki 2020-02-17T10:52:03Z 2020-02-17T10:52:03Z 2019-02
dc.identifier.citation 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 .
dc.identifier.other PURE: 128364489
dc.identifier.other PURE UUID: 38e738d8-f3e5-4dfa-8edb-307a1cab2b0c
dc.identifier.other WOS: 000457454000008
dc.identifier.other ORCID: /0000-0002-1340-9732/work/70948424
dc.identifier.other ORCID: /0000-0003-0521-5062/work/85521587
dc.description.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. en
dc.format.extent 17
dc.language.iso eng
dc.relation.ispartof Molecular & Cellular Proteomics
dc.rights cc_by
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject INTEGRIN ALPHA-6-BETA-4
dc.subject PROTEINS
dc.subject BETA-4
dc.subject POLARITY
dc.subject ADHESION
dc.subject COMPLEX
dc.subject CELLS
dc.subject 1182 Biochemistry, cell and molecular biology
dc.title Assembly of the beta 4-Integrin Interactome Based on Proximal Biotinylation in the Presence and Absence of Heterodimerization en
dc.type Article
dc.contributor.organization Institute of Biotechnology
dc.contributor.organization Doctoral Programme in Integrative Life Science
dc.contributor.organization Doctoral Programme in Drug Research
dc.contributor.organization Doctoral Programme in Biomedicine
dc.contributor.organization University Management
dc.contributor.organization Molecular Systems Biology
dc.description.reviewstatus Peer reviewed
dc.relation.issn 1535-9476
dc.rights.accesslevel openAccess
dc.type.version publishedVersion

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