eLife:细胞调控分泌蛋白磷酸化新机制

2015-03-23 佚名 生物谷

近日,美国加州大学圣地亚哥分校的研究人员在国际期刊elife在线发表了他们关于细胞通过分泌途径调控胞外蛋白磷酸化相关分子机制的最新研究进展。 研究人员指出,之前研究已经发现胞外存在大量磷酸化蛋白,但通过分泌途径发挥激酶活性的磷酸激酶直到最近才被发现,目前对此类磷酸激酶调控作用的相关研究仍较少。Fam20C是位于高尔基体上的一种酪蛋白激酶,能够对多种分泌蛋白进行磷酸化并且对适当的生物矿化作用至关重要

近日,美国加州大学圣地亚哥分校的研究人员在国际期刊elife在线发表了他们关于细胞通过分泌途径调控胞外蛋白磷酸化相关分子机制的最新研究进展。

研究人员指出,之前研究已经发现胞外存在大量磷酸化蛋白,但通过分泌途径发挥激酶活性的磷酸激酶直到最近才被发现,目前对此类磷酸激酶调控作用的相关研究仍较少。Fam20C是位于高尔基体上的一种酪蛋白激酶,能够对多种分泌蛋白进行磷酸化并且对适当的生物矿化作用至关重要。

Fam20A是Fam20C的一种类似物,在釉质形成过程中发挥重要作用,但Fam20A的生化功能仍不清楚。研究人员发现Fam20A能够增强Fam20C的激酶活性,促进釉基质蛋白的磷酸化。Fam20A是一种假激酶,能够与Fam20C形成功能性复合物,这种复合物会通过分泌途径增强胞外蛋白磷酸化。

这项研究揭示了Fam20C与Fam20A协同调控釉质形成的分子机制,并为通过分泌途径调控胞外蛋白磷酸化相关研究提供了重要启示。

原始出处:

Jixin Cui, Junyu Xiao, Vincent S Tagliabracci, Jianzhong Wen, Meghdad Rahdar, Jack E Dixon.A secretory kinase complex regulates extracellular protein phosphorylation[J].eLIFE.March 19, 2015.

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    2015-10-16 膀胱癌
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    2016-02-23 clmlylxy
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    2015-06-26 gwc392