In Candida albicans hyphae, Sec2p is physically associated with SEC2 mRNA on secretory vesicles.
In Candida albicans hyphae, Sec2p is physically associated with SEC2 mRNA on secretory vesicles.
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DOI：
10.1111/mmi.12799
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发表时间：
2014-11
影响因子：
3.6
通讯作者：
Sudbery PE
中科院分区：
文献类型：
--
作者：
Caballero-Lima D;Hautbergue GM;Wilson SA;Sudbery PE
白色念珠菌菌丝从其尖端以高度极化的方式生长。这种极化生长需要分泌囊泡不断地输送到尖端区域。囊泡的递送取决于Sec2p，兔GTPase Sec4p的鸟嘌呤交换因子（GEF）。GTP结合的Sec4p是分泌囊泡从反式高尔基体转移到极化生长位点所必需的。我们之前的研究表明，Sec2p残基S584的磷酸化对于Sec2p支持菌丝是必要的，而不是酵母生长。我们发现在分泌囊中，SEC2 mRNA与Sec2p存在物理关联。此外，我们发现S584的磷酸化允许SEC2 mRNA与Sec2p分离，我们推测这是Sec2p功能和/或翻译所必需的。在菌丝延伸过程中，生长端与细胞核的距离可达15 μm。SEC2 mRNA在分泌囊泡上转运到尖端，使SEC2翻译定位到尖端，从而使该关键蛋白在极化生长部位充分积累。
Candida albicans hyphae grow in a highly polarized fashion from their tips. This polarized growth requires the continuous delivery of secretory vesicles to the tip region. Vesicle delivery depends on Sec2p, the Guanine Exchange Factor (GEF) for the Rab GTPase Sec4p. GTP bound Sec4p is required for the transit of secretory vesicles from the trans-Golgi to sites of polarized growth. We previously showed that phosphorylation of Sec2p at residue S584 was necessary for Sec2p to support hyphal, but not yeast growth. Here we show that on secretory vesicles SEC2 mRNA is physically associated with Sec2p. Moreover, we show that the phosphorylation of S584 allows SEC2 mRNA to dissociate from Sec2p and we speculate that this is necessary for Sec2p function and/or translation. During hyphal extension, the growing tip may be separated from the nucleus by up to 15 μm. Transport of SEC2 mRNA on secretory vesicles to the tip localizes SEC2 translation to tip allowing a sufficient accumulation of this key protein at the site of polarized growth.
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