The yeast cell wall integrity pathway signals from recycling endosomes upon elimination of phosphatidylinositol (4,5)-bisphosphate by mammalian phosphatidylinositol 3-kinase.
作者： Teresa Fernández-Acero , Isabel Rodríguez-Escudero , María Molina , Víctor J. Cid
DOI: 10.1016/J.CELLSIG.2015.08.004
关键词:
摘要: Phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P(2)] is essential for recognition of the plasma membrane inner leaf by protein complexes. We expressed mammalian class I phosphoinositide 3-kinase (PI3K) in Saccharomyces cerevisiae to eliminate PtdIns(4,5)P(2) its conversion into PtdIns(3,4,5)P(3), a lipid naturally missing this yeast. This led loss actin function and endocytosis defects, causing blockage polarized secretion. Also, cell wall integrity (CWI) mitogen-activated kinase (MAPK) pathway was activated, triggering typical transcriptional response. In absence at membrane, Pkc1 upstream CWI MAPK module localized post-Golgi endosomes marked SNARE Snc1 Rab GTPases Ypt31 Ypt32. Other components head pathway, like mechanosensor Wsc1, GTPase Rho1 activator GDP/GTP exchange factor Rom2, co-localized with these compartments. Chemical inhibition PI3K proved that both activation relocation are reversible. These results suggest able respond identity from recycling endosomes.
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