Dual acylation of the 45 kDa gliding-associated protein (GAP45) in Plasmodium falciparum merozoites
Dual acylation of the 45 kDa gliding-associated protein (GAP45) in Plasmodium falciparum merozoites
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DOI：
10.1016/j.molbiopara.2006.04.008
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发表时间：
2006-09-01
影响因子：
1.5
通讯作者：
Holder, Anthony A.
中科院分区：
文献类型：
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作者：
Rees-Channer, Roxanne R.;Martin, Stephen R.;Holder, Anthony A.
滑行运动对于弓形虫速殖子[1]和疟原虫子孢子[2]成功入侵宿主细胞是必不可少的，尽管疟原虫spp.裂殖子似乎不表现出滑动运动，它们主动地附着和入侵红细胞(在[3]中回顾)。驱动滑行运动和宿主细胞入侵的潜在力量与位于寄生虫质膜和内膜复合体(IMC)之间的肌球蛋白马达有关[4]。肌球蛋白属于一个不同的类别(XIV型)[5]，称为肌球蛋白A(MyoA)。弓形虫MyoA被发现与一种名为肌球蛋白轻链1(MLC1)的蛋白质共同纯化[6]。在疟原虫子孢子[7]和裂殖子[8，9]中已鉴定出该蛋白的同源蛋白，称为肌球蛋白尾部结构域相互作用蛋白(MTIP)。最近的证据表明，MyoA通过一种蛋白质中间体锚定在IMC的外表面，尽管MTIP最初被认为参与了在IMC锚定这一复合体，但它如何介导这一功能尚不清楚。在弓形虫中，发现了两个新的连接发动机和IMC的候选蛋白，即45和50 kDa的滑动相关蛋白(GAP45和GAP50)，它们同时与MLC1和MyoA形成复合体，为MyoA在IMC中提供了一个刚性锚定[10]。弓形虫(Tg)GAP50被认为是该复合体的跨膜受体，但TgGAP45的确切作用尚不清楚。在疟原虫中也发现了GAP45和GAP50[9]。在这里我们缩写：GAP，滑动相关蛋白；IMC，内膜复合体；MLC1，肌球蛋白轻链1；MTIP，肌球蛋白尾部结构域相互作用蛋白；MyoA，肌球蛋白A；NMT，N-肉豆蔻酰转移酶∗通讯作者。电话：+44 20 8816 2402；传真：+44 20 8816 2730。电邮地址：rrees@nimr。MRC.交流电。英国(RR Rees-Channer)。检查GAP45的生物合成，并确定肉豆蔻酰化和棕榈酰化都是该蛋白潜在的重要修饰。
Gliding motility is essential for successful host cell invasion by both Toxoplasma gondii tachyzoites [1] a nd Plasmodium sporozoites [2], and although Plasmodium spp. merozoites do not appear to display gliding motility, they actively attach to and invade erythrocytes (reviewed in [3]). The underlying force driving both gliding motility and host cell invasion has been linked to an acto-myosin motor that is located in the space between the parasite’s plasma membrane and inner membrane complex (IMC)[4]. The myosin belongs to a distinct class (type XIV)[5] a nd is called myosin A (MyoA). T. gondii MyoA was found to co-purify with a protein designated Myosin Light Chain 1 (MLC1)[6]. An orthologue of this protein named Myosin Tail domain Interacting Protein (MTIP) has been identified in Plasmodium sporozoites [7] and merozoites [8, 9]. Recent evidence suggests that MyoA is anchored at the outer face of the IMC by means of a protein intermediate and although MTIP was initially suggested to be involved in anchoring this complex at the IMC, how it would mediate this function is unclear. Two new candidates for linking the motor to the IMC, the 45 and 50 kDa gliding-associated proteins (GAP45 and GAP50) were identified in complex with both MLC1 and MyoA in T. gondii, providing a rigid anchorage for MyoA in the IMC [10]. T. gondii (Tg) GAP50 was proposed to be the transmembrane receptor for the complex but the exact role of TgGAP45 is unknown. GAP45 and GAP50 have also been identified in Plasmodium [9]. Here weAbbreviations: GAP, gliding-associated protein; IMC, inner membrane complex; MLC1, myosin light chain 1; MTIP, myosin tail domain interacting protein; MyoA, myosin A; NMT, N-myristoyl transferase∗ Corresponding author. Tel.:+ 44 20 8816 2402; fax:+ 44 20 8816 2730. E-mail address: rrees@ nimr. mrc. ac. uk (RR Rees-Channer). examine the biosynthesis of GAP45 and identify acylation by both myristoylation and palmitoylation as potentially important modifications of this protein.