Díaz Añel Alberto M
Center for Molecular Genetics, University of California at San Diego, San Diego, CA, USA.
Biochem J. 2007 Aug 15;406(1):157-65. doi: 10.1042/BJ20070359.
The requirement of DAG (diacylglycerol) to recruit PKD (protein kinase D) to the TGN (trans-Golgi network) for the targeting of transport carriers to the cell surface, has led us to a search for new components involved in this regulatory pathway. Previous findings reveal that the heterotrimeric Gbetagamma (GTP-binding protein betagamma subunits) act as PKD activators, leading to fission of transport vesicles at the TGN. We have recently shown that PKCeta (protein kinase Ceta) functions as an intermediate member in the vesicle generating pathway. DAG is capable of activating this kinase at the TGN, and at the same time is able to recruit PKD to this organelle in order to interact with PKCeta, allowing phosphorylation of PKD's activation loop. The most qualified candidates for the production of DAG at the TGN are PI-PLCs (phosphatidylinositol-specific phospholipases C), since some members of this family can be directly activated by Gbetagamma, utilizing PtdIns(4,5)P2 as a substrate, to produce the second messengers DAG and InsP3. In the present study we show that betagamma-dependent Golgi fragmentation, PKD1 activation and TGN to plasma membrane transport were affected by a specific PI-PLC inhibitor, U73122 [1-(6-{[17-3-methoxyestra-1,3,5(10)-trien-17-yl]amino}hexyl)-1H-pyrrole-2,5-dione]. In addition, a recently described PI-PLC activator, m-3M3FBS [2,4,6-trimethyl-N-(m-3-trifluoromethylphenyl)benzenesulfonamide], induced vesiculation of the Golgi apparatus as well as PKD1 phosphorylation at its activation loop. Finally, using siRNA (small interfering RNA) to block several PI-PLCs, we were able to identify PLCbeta3 as the sole member of this family involved in the regulation of the formation of transport carriers at the TGN. In conclusion, we demonstrate that fission of transport carriers at the TGN is dependent on PI-PLCs, specifically PLCbeta3, which is necessary to activate PKCeta and PKD in that Golgi compartment, via DAG production.
二酰基甘油(DAG)需要将蛋白激酶D(PKD)募集到反式高尔基体网络(TGN),以便将运输载体靶向细胞表面,这促使我们寻找参与该调节途径的新成分。先前的研究结果表明,异源三聚体Gβγ(GTP结合蛋白βγ亚基)作为PKD激活剂,导致TGN处运输小泡的裂变。我们最近表明,蛋白激酶Cε(PKCε)在小泡生成途径中起中间成员的作用。DAG能够在TGN处激活这种激酶,同时能够将PKD募集到这个细胞器,以便与PKCε相互作用,使PKD的激活环磷酸化。在TGN处产生DAG的最有可能的候选者是磷脂酰肌醇特异性磷脂酶C(PI-PLC),因为该家族的一些成员可以被Gβγ直接激活,利用磷脂酰肌醇-4,5-二磷酸(PtdIns(4,5)P2)作为底物,产生第二信使DAG和肌醇-1,4,5-三磷酸(InsP3)。在本研究中,我们表明,βγ依赖性高尔基体碎片化、PKD1激活以及从TGN到质膜的运输受到特异性PI-PLC抑制剂U73122 [1-(6-{[17-3-甲氧基雌甾-1,3,5(10)-三烯-17-基]氨基}己基)-1H-吡咯-2,5-二酮]的影响。此外,最近描述的一种PI-PLC激活剂,间-3M3FBS [2,4,6-三甲基-N-(间-三氟甲基苯基)苯磺酰胺],诱导高尔基体囊泡化以及PKD1在其激活环处的磷酸化。最后,使用小干扰RNA(siRNA)阻断几种PI-PLC,我们能够确定磷脂酶Cβ3(PLCβ3)是该家族中参与调节TGN处运输载体形成的唯一成员。总之,我们证明TGN处运输载体的裂变依赖于PI-PLC,特别是PLCβ3,它通过产生DAG在该高尔基体区室中激活PKCε和PKD是必需的。