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Lsp1 partially substitutes for Pil1 function in eisosome assembly under stress conditions
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SYSNO ASEP 0576685 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Lsp1 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, ORCIDČíslo článku jcs260554 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. slova KEY WORDS ; Eisosome ; Membrane compartment of Can1 ; Sphingolipid ; Stress ; Pil1 ; Lsp1 Obor OECD Cell biology CEP GA20-04987S GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora UEM-P - RVO:68378041 UT WOS 000971896200001 EID SCOPUS 85147458381 DOI https://doi.org/10.1242/jcs.260554 Anotace Eisosomes 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. Pracoviště Ústav experimentální medicíny Kontakt Arzuv Čaryjeva, arzuv.caryjeva@iem.cas.cz, Tel.: 241 062 218, 296 442 218 Rok sběru 2024 Elektronická adresa https://journals.biologists.com/jcs/article/136/3/jcs260554/286927/Lsp1-partially-substitutes-for-Pil1-function-in
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