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作 者:Ting Ma Jun-Ru Tan Jin-Yu Lu Sha Li Yan Zhang
机构地区:[1]College of Life Sciences,Shandong Agricultural University,Taian,Shandong 271018,China [2]Frontiers Science Center for Cell Responses,College of Life Sciences,Nankai University,Tianjin 300071,China
出 处:《Journal of Genetics and Genomics》2024年第10期1079-1088,共10页遗传学报(英文版)
基 金:This work is supported by National Natural Science Foundation of China(31970332).
摘 要:Hetero-tetrameric soluble N-ethylmaleimide-sensitive factor attachment protein receptors(SNAREs)complexes are critical for vesicle-target membrane fusion within the endomembrane system of eukaryotic cells.SNARE assembly involves four different SNARE motifs,Qa,Qb,Qc,and R,providedby three orfour SNARE proteins.YKT6 is an atypical R-SNARE that lacks a transmembrane domain and is involved in multiple vesicle-target membrane fusions.Although YKT6 is evolutionarily conserved and essential,its function and regulation in different phyla seem distinct.Arabidopsis YKT61,the yeast and metazoan YKT6 homologue,is essential for gametophytic development,plays a critical role in sporophytic cells,and me-diates multiple vesicle-target membrane fusion.However,its molecular regulation is unclear.We report here that YKT61 is S-acylated.Abolishing its S-acylation by a C195S mutation dissociates YKT61 from endomembrane structures and causes its functional loss.Although interacting with various SNARE pro-teins,YKT61functions not as a canonical R-SNAREbut coordinates with otherR-SNAREs to participate in theformationof SNAREcomplexes.Phylum-specific molecular regulation of YKT6 may be evolvedto allow more efficient SNARE assembly in different eukaryotic cells.
关 键 词:Longin domain S-ACYLATION Vesicle trafficking R-SNARE Arabidopsis thaliana
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