Počet záznamů: 1  

Lsp1 partially substitutes for Pil1 function in eisosome assembly under stress conditions

  1. 1.
    SYSNO ASEP0576685
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevLsp1 partially substitutes for Pil1 function in eisosome assembly under stress conditions
    Tvůrce(i) Veselá, Petra (UEM-P) RID, ORCID
    Zahumenský, Jakub (UEM-P) ORCID, RID
    Malínský, Jan (UEM-P) RID, ORCID
    Číslo článkujcs260554
    Zdroj.dok.Journal of Cell Science. - : Company of Biologists - ISSN 0021-9533
    Roč. 136, č. 3 (2023)
    Poč.str.14 s.
    Jazyk dok.eng - angličtina
    Země vyd.GB - Velká Británie
    Klíč. slovaKEY WORDS ; Eisosome ; Membrane compartment of Can1 ; Sphingolipid ; Stress ; Pil1 ; Lsp1
    Obor OECDCell biology
    CEPGA20-04987S GA ČR - Grantová agentura ČR
    Způsob publikováníOpen access
    Institucionální podporaUEM-P - RVO:68378041
    UT WOS000971896200001
    EID SCOPUS85147458381
    DOI https://doi.org/10.1242/jcs.260554
    AnotaceEisosomes are large hemitubular structures that underlie the invaginated microdomains in the plasma membrane of various ascomycetous fungi, lichens and unicellular algae. In fungi, they are organized by BAR-domain containing proteins of the Pil1 family. Two such proteins, Pil1 and Lsp1, participate in eisosome formation in the yeast Saccharomyces cerevisiae. Under normal laboratory conditions, deletion of the PIL1 gene results in the inability of cells to assemble wild-type-like eisosomes. We found that under certain stress conditions, Lsp1 partially substitutes for the Pil1 function and mediates assembly of eisosomes, specifically following a decrease in the activity of serine palmitoyltransferase, for example, in response to hyperosmotic stress. Besides Lsp1, the assembly of eisosomes lacking Pil1 also requires Seg1 and Nce102 proteins. Using next -generation sequencing, we found that the seg1Ance102Apil1A strain, which is unable to form eisosomes, overexpresses genes coding for proteins of oxidative phosphorylation and tricarboxylic acid cycle. By contrast, genes involved in DNA repair, ribosome biogenesis and cell cycle are downregulated. Our results identify Lsp1 as a stress -responsive eisosome organizer and indicate several novel functional connections between the eisosome and essential cellular processes.
    PracovištěÚstav experimentální medicíny
    KontaktArzuv Čaryjeva, arzuv.caryjeva@iem.cas.cz, Tel.: 241 062 218, 296 442 218
    Rok sběru2024
    Elektronická adresahttps://journals.biologists.com/jcs/article/136/3/jcs260554/286927/Lsp1-partially-substitutes-for-Pil1-function-in
Počet záznamů: 1  

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