Plant J: 中美油菜科研团队共同揭示与非特异性磷脂酶 C4的酰化作用决定了其在植物对缺磷反应中的作用
非特异性磷脂酶 c (NPC)参与植物的生长发育和胁迫反应。为了阐明 npc 介导细胞功能的机制，我们发现 NPC4在 c 末端是 s 酰化的，酰化决定了它的质膜结合和功能。利用拟南芥 NPC4分离株检测 NPC4的酰化作用，并在体外重组 NPC4。C 末端 Cys-533为 s 酰化残基，NPC4(NPC4C533A)中 Cys-533突变为 Ala-533，导致 NPC4的 s 酰化和膜结合缺失。NPC4基因的敲除阻碍了磷酸磷脂糖基肌醇磷酰神经酰胺(GIPC)在缺磷状态下的降解，而 NPC4C533A 基因的引入未能弥补这一缺陷，从而支持了非酰基化 NPC4C533A 在缺磷状态下不能水解 GIPC 的假说。此外，NPC4C533A 在胁迫条件下不能补充 npc4-1的初生根生长。此外，NPC4在甘蓝型油菜中是 s 酰化的，bnac01的 s 酰化半胱氨酸残基发生突变，导致 s 酰化及其膜结合的丢失。
总之，我们的结果表明，NPC4在 c 端的 s 酰化是保守的，它的膜缔合、磷酸磷脂水解和植物逆境反应的功能需要。
Non‐specific phospholipase C (NPC) is involved in plant growth, development and stress responses. To elucidate the mechanism by which NPCs mediate cellular functions, here we show that NPC4 is S‐acylated at the C terminus and that acylation determines its plasma membrane (PM) association and function. The acylation of NPC4 was detected using NPC4 isolated from Arabidopsis and reconstituted in vitro. The C‐terminal Cys‐533 was identified as the S‐acylation residue, and the mutation of Cys‐533 to Ala‐533 in NPC4 (NPC4C533A) led to the loss of S‐acylation and membrane association of NPC4. The knockout of NPC4 impeded the phosphate deficiency‐induced decrease of the phosphosphingolipid glycosyl inositol phosphoryl ceramide (GIPC), but introducing NPC4C533A to npc4‐1 failed to complement this defect, thereby supporting the hypothesis that the non‐acylated NPC4C533A fails to hydrolyze GIPC during phosphate deprivation. Moreover, NPC4C533A failed to complement the primary root growth in npc4‐1 under stress. In addition, NPC4 in Brassica napus was S‐acylated and mutation of the S‐acylating cysteine residue of BnaC01.NPC4 led to the loss of S‐acylation and its membrane association. Together, our results reveal that S‐acylation of NPC4 in the C terminus is conserved and required for its membrane association, phosphosphingolipid hydrolysis and function in plant stress responses.
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