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首页> 外文期刊>Journal of Cell Science >Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.
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Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.

机译：尾锚（TA）蛋白质膜插入的不同靶向途径。

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摘要

Tail-anchored (TA) proteins are characterised by a C-terminal transmembrane region that mediates post-translational insertion into the membrane of the endoplasmic reticulum (ER). We have investigated the requirements for membrane insertion of three TA proteins, RAMP4, Sec61beta and cytocrome b5. We show here that newly synthesised RAMP4 and Sec61beta can accumulate in a cytosolic, soluble complex with the ATPase Asna1 before insertion into ER-derived membranes. Membrane insertion of these TA proteins is stimulated by ATP, sensitive to redox conditions and blocked by alkylation of SH groups by N-ethylmaleimide (NEM). By contrast, membrane insertion of cytochrome b5 is not found to be mediated by Asna1, not stimulated by ATP and not affected by NEM or an oxidative environment. The Asna1-mediated pathway of membrane insertion of RAMP4 and Sec61beta may relate to functions of these proteins in the ER stress response.
机译：尾锚定（TA）蛋白的特征是C端跨膜区介导翻译后插入内质网（ER）膜中。我们已经研究了三种TA蛋白，RAMP4，Sec61beta和crocrocrome b5的膜插入要求。我们在这里显示，新合成的RAMP4和Sec61beta可以在插入ER来源的膜之前与ATPase Asna1一起在胞质，可溶性复合物中积累。这些TA蛋白的膜插入受到ATP的刺激，对氧化还原条件敏感，并被N-乙基马来酰亚胺（NEM）的SH基团烷基化所阻止。相反，未发现细胞色素b5的膜插入是由Asna1介导的，不受ATP刺激的，不受NEM或氧化环境的影响。 Asna1介导的RAMP4和Sec61beta的膜插入途径可能与这些蛋白质在ER应激反应中的功能有关。

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