Inner nuclear membrane proteins Lem2 and Bqt4 interact with different lipid synthesis enzymes in fission yeast
Inner nuclear membrane proteins Lem2 and Bqt4 interact with different lipid synthesis enzymes in fission yeast
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核膜蛋白 Lem2 和 Bqt4 与裂殖酵母中不同的脂质合成酶相互作用
DOI：
10.1093/jb/mvad017
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发表时间：
2023
期刊：
影响因子：
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通讯作者：
Hiraoka Yasushi
中科院分区：
文献类型：
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作者：
Hirano Yasuhiro;Kinugasa Yasuha;Kubota Yoshino;Obuse Chikashi;Haraguchi Tokuko;Hiraoka Yasushi
核膜（NE）是由内膜和外膜组成的双膜结构，其在空间上将细胞核与细胞质分开，并且其功能对于细胞功能如基因组维持至关重要。在裂殖酵母裂殖酵母中，内核膜蛋白Lem2和Bqt4在维持NE结构中起关键作用。我们以前发现，双缺失oflem 2+和bqt 4+导致合成的致命缺陷与严重的NE破裂，和Elo2，一个单独的极长链脂肪酸延长酶的过度表达，抑制这种缺陷通过恢复NE。然而，这种修复的分子基础仍然难以捉摸。为了解决这个问题，我们在这项研究中通过免疫沉淀和质谱鉴定了Lem2和Bqt4结合蛋白。45和23蛋白被确定为Lem2和Bqt4结合蛋白，分别。虽然这些结合蛋白部分重叠，Lem2和Bqt4与不同类型的脂质代谢酶相互作用：Cho2，Ole1和Erg11的Lem2和Cwh43的Bqt4。已知这些酶参与各种脂质合成过程，这表明Lem2和Bqt4可能通过与这些酶结合来调节脂质合成。
The nuclear envelope (NE) is a double-membrane structure consisting of inner and outer membranes that spatially separate the nucleus from the cytoplasm, and its function is critical for cellular functions such as genome maintenance. In the fission yeast,Schizosaccharomyces pombe, the inner nuclear membrane proteins, Lem2 and Bqt4, play pivotal roles in maintaining the NE structure. We previously found that the double deletion oflem2+andbqt4+causes a synthetic lethal defect associated with severe NE rupture, and overexpression of Elo2, a solo very-long-chain fatty acid elongase, suppresses this defect by restoring the NE. However, the molecular basis of this restoration remains elusive. To address this, we identified Lem2- and Bqt4-binding proteins via immunoprecipitation and mass spectrometry in this study. Forty-five and 23 proteins were identified as Lem2- and Bqt4-binding proteins, respectively. Although these binding proteins partially overlapped, Lem2 and Bqt4 interacted with different types of lipid metabolic enzymes: Cho2, Ole1 and Erg11 for Lem2 and Cwh43 for Bqt4. These enzymes are known to be involved in various lipid synthesis processes, suggesting that Lem2 and Bqt4 may contribute to the regulation of lipid synthesis by binding to these enzymes.