Number of the records: 1  

Flotillins, Erlins, and HIRs: From Animal Base Camp to Plant New Horizons

  1. 1.
    SYSNO ASEP0473314
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleFlotillins, Erlins, and HIRs: From Animal Base Camp to Plant New Horizons
    Author(s) Daněk, Michal (UEB-Q) ORCID
    Valentová, O. (CZ)
    Martinec, Jan (UEB-Q) RID, ORCID
    Number of authors3
    Source TitleCritical Reviews in Plant Sciences - ISSN 0735-2689
    Roč. 35, č. 4 (2016), s. 191-214
    Number of pages24 s.
    Languageeng - English
    CountryUS - United States
    KeywordsArabidopsis thaliana ; erlin ; flotillin ; hir ; membrane microdomains ; SPFH domain
    Subject RIVCE - Biochemistry
    R&D ProjectsGA14-09685S GA ČR - Czech Science Foundation (CSF)
    Institutional supportUEB-Q - RVO:61389030
    UT WOS000398201200001
    EID SCOPUS84994882457
    DOI10.1080/07352689.2016.1249690
    AnnotationPlant stomatin/prohibitin/flotillin/HflK/C (SPFH) proteins are represented by prohibitins, flotillins, stomatins, erlins, and hypersensitive induced reaction proteins (HIRs). The purpose of this review is to summarize the current state of knowledge regarding plant flotillins and HIRs and to assign putative functions of plant flotillins and erlins based on the known functions of their mammalian homologs. Similar to human flotillins, plant flotillins are localized in membrane microdomains, and involved in endocytosis, and interact with receptor kinases. HIRs play an important role in plant immunity by promoting the hypersensitive response and binding to leucine-rich repeat proteins. In this way, they participate in resistance to bacterial or fungal pathogens. We further focused on flotillins, HIRs, and erlins in Arabidopsis thaliana and, using public databases, described them in terms of the following: 1) their transcription throughout plant ontogeny and under various environmental conditions; 2) the presence of conserved domains or characteristic motifs in their amino acid sequences; and 3) their potential interactions with other proteins. Based on these data, we hypothesize about their additional functions and properties.
    WorkplaceInstitute of Experimental Botany
    ContactDavid Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469
    Year of Publishing2017
Number of the records: 1  

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