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首页> 外文期刊>Biochimica et Biophysica Acta. Molecular and cell biology of Lipids >Yeast phosphatidylinositol transfer protein Pdr17 does not require high affinity phosphatidylinositol binding for its cellular function
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Yeast phosphatidylinositol transfer protein Pdr17 does not require high affinity phosphatidylinositol binding for its cellular function

机译：酵母磷脂酰肌醇转移蛋白PDR17不需要高亲和力磷脂酰肌醇结合其细胞功能

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摘要

Yeast phosphatidylinositol transfer protein (PITP) Pdr17 is an essential component of the complex required for decarboxylation of phosphatidylserine (PS) to phosphatidylethanolamine (PE) at a non-mitochondrial location. According to current understanding, this process involves the transfer of PS from the endoplasmic reticulum to the Golgi/endosomes. We generated a Pdr17(E237A, K269A) mutant protein to better understand the mechanism by which Pdr17p participates in the processes connected to the decarboxylation of PS to PE. We show that the Pdr17(E237A, K269A) mutant protein is not capable of binding phosphatidylinositol (PI) using permeabilized human cells, but still retains the ability to transfer PI between two membrane compartments in vitro. We provide data together with molecular models showing that the mutations E237A and K269A changed only the lipid binding cavity of Pdr17p and not its surface properties. In contrast to Pdr16p, a close homologue, the ability of Pdr17p to bind PI is not required for its major cellular function in the inter-membrane transfer of PS. We hypothesize that these two closely related yeast PITPs, Pdr16p and Pdr17p, have evolved from a common ancestor. Pdr16p fulfills those role(s) in which the ability to bind and transfer PI is required, while Pdr17p appears to have adapted to a different role which does not require the high affinity binding of PI, although the protein retains the capacity to transfer PI. Our results indicate that PITPs function in complex ways in vivo and underscore the need to consider multiple PITP parameters when studying these proteins in vitro.
机译：酵母磷脂酰肌醇转移蛋白（PITP）PDR17是在非线粒体位置在非线粒体位置磷酸三烷基酮（PS）脱羧至磷脂酰乙醇胺（PE）所需的复合物所需的基本组分。根据目前的理解，该方法涉及将Ps从内质网转移到Golgi / endosomes。我们产生了PDR17（E237A，K269A）突变蛋白，以更好地理解PDR17P参与与PS的脱羧的方法的机制。我们表明PDR17（E237A，K269A）突变蛋白不能使用透化的人细胞结合磷脂酰肌醇（PI），但仍然保留在体外两个膜隔室之间转移PI的能力。我们将数据与分子模型一起提供数据，表明突变E237A和K269A仅改变PDR17P的脂质结合腔而不是其表面​​性质。与PDR16P相反，密闭同源物，PDR17P在PS的​​膜间转移中的主要细胞功能不需要PDR17P与结合PI的能力。我们假设这两个密切相关的酵母PICP，PDR16P和PDR17P已经从共同的祖先演变。 PDR16P符合那些需要结合和转移PI的能力，而PDR17P似乎适应不需要PI的高亲和力结合的不同作用，尽管蛋白质保留转移PI的能力。我们的结果表明，在体内的复杂方法中，PICPS功能在体外研究这些蛋白质时需要考虑多种PITP参数。

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