Gpn1 and Gpn3 associate tightly and their protein levels are mutually dependent in mammalian cells
作者:, Mónica R. Calera
摘要:Abstract Gpn1 and Gpn3 are GTPases individually required for nuclear targeting of RNA polymerase II. Here we show that whereas Gpn3-EYFP distributed between the cytoplasm and cell nucleus, it was mainly cytoplasmic when coexpressed with Gpn1-Flag. Gpn3-Flag retained Gpn1-EYFP in the cytoplasm. However, Gpn3-EYFP/Gpn1-Flag nucleocytoplasmic shuttling was revealed after inhibiting nuclear export with leptomycin B. All Gpn3-EYFP coimmunoprecipitated with Gpn1-Flag, and all Gpn1-EYFP with Gpn3-Flag. Importantly, most endogenous Gpn1 and Gpn3 also associate. Gpn1–Gpn3 interaction was essential to maintain steady-state protein levels of both GTPases. We propose that most Gpn1 and Gpn3 associate, are mobilized, and function as a protein complex.
关键词:Gpn1; Gpn3; Gpn1–Gpn3 interaction; Gpn1–Gpn3 nucleocytoplasmic shuttling; Interdependent protein levels; shRNA
论文方向:[{"id":13,"name":"细胞生物学"},{"id":879,"name":"生物化学"}]
发表期刊:FEBS Letters Volume 588, Issue 21
发表时间:Mon Nov 03 00:00:00 CST 2014
数字识别码:10.1016/j.febslet.2014.08.038
是否作者本人: 否
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