Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development.
Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development.
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非洲爪蟾发育过程中磷脂酶 C 和 D 对 Src、钙释放和膜融合的调节。
DOI：
10.1016/j.ydbio.2015.02.020
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发表时间：
2015
影响因子：
2.7
通讯作者：
Stith,BradleyJ
中科院分区：
文献类型：
--
作者：
Stith,BradleyJ
本文综述了脂质如何调节膜融合和参与三个发育阶段的蛋白：卵母细胞成熟到受精卵、受精和第一次卵裂。几十年的研究表明，磷脂酸（PA）在细胞内释放钙，最近的研究表明，这种脂质可以在爪蟾受精过程中激活Src酪氨酸激酶或磷脂酶C。大量的报告总结显示，在三个不同的发育阶段，脂质第二信使肌醇1,4,5-三磷酸和sn 1,2-二酰基甘油（DAG）有三个水平的增加。此外，还讨论了PA、神经酰胺、溶血磷脂酰胆碱、磷脂原、磷脂酰肌醇4-磷酸、磷脂酰肌醇5-磷酸、磷脂酰肌醇4,5-二磷酸、膜微结构域（筏）和磷脂酰肌醇3,4,5-三磷酸在调节膜融合（顶体反应、精卵融合、皮质颗粒胞吐）、肌醇1,4,5-三磷酸受体和钙释放中的可能作用。本文还讨论了六种脂肪酶在受精过程中产生脂质第二信使的作用：磷脂酶D、autotaxin、脂素1、鞘磷脂酶、磷脂酶C和磷脂酶A2。更具体地说，参与发育事件的蛋白质及其通过脂质结合到SH3， SH4， PH， PX或C2蛋白结构域的调节被强调。提出了PA激活Src的新模型（通过SH3、SH4和一个独特的结构域），这可能是为什么爪蟾受精不需要PLCγ的SH2结构域，PA激活磷脂酶C， PA在受精后的钙波中发挥作用，以及钙/钙调蛋白可能是受精后筏中Src损失的原因。还讨论了受精过程中DAG的大量增加源于PA的磷脂酶D的产生和脂质对DAG的去磷酸化。
This review emphasizes how lipids regulate membrane fusion and the proteins involved in three developmental stages: oocyte maturation to the fertilizable egg, fertilization and during first cleavage. Decades of work show that phosphatidic acid (PA) releases intracellular calcium, and recent work shows that the lipid can activate Src tyrosine kinase or phospholipase C during Xenopus fertilization. Numerous reports are summarized to show three levels of increase in lipid second messengers inositol 1,4,5-trisphosphate and sn 1,2-diacylglycerol (DAG) during the three different developmental stages. In addition, possible roles for PA, ceramide, lysophosphatidylcholine, plasmalogens, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 4,5-bisphosphate, membrane microdomains (rafts) and phosphatidylinositol 3,4,5-trisphosphate in regulation of membrane fusion (acrosome reaction, sperm–egg fusion, cortical granule exocytosis), inositol 1,4,5-trisphosphate receptors, and calcium release are discussed. The role of six lipases involved in generating putative lipid second messengers during fertilization is also discussed: phospholipase D, autotaxin, lipin1, sphingomyelinase, phospholipase C, and phospholipase A2. More specifically, proteins involved in developmental events and their regulation through lipid binding to SH3, SH4, PH, PX, or C2 protein domains is emphasized. New models are presented for PA activation of Src (through SH3, SH4 and a unique domain), that this may be why the SH2 domain of PLCγ is not required for Xenopus fertilization, PA activation of phospholipase C, a role for PA during the calcium wave after fertilization, and that calcium/calmodulin may be responsible for the loss of Src from rafts after fertilization. Also discussed is that the large DAG increase during fertilization derives from phospholipase D production of PA and lipin dephosphorylation to DAG.