Gpn1 and Gpn3 associate tightly and their protein levels are mutually dependent in mammalian cells |
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| Authors: | Lucía E Méndez-Hernández Ana E Pérez-Mejía Bárbara Lara-Chacón Angel A Barbosa-CamachoSonia G Peña-Gómez Mayra Martínez-SánchezAngélica Y Robledo-Rivera Roberto Sánchez-Olea Mónica R Calera |
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| Institution: | Instituto de Física, Universidad Autónoma de San Luis Potosí, Manuel Nava 6, Zona Universitaria, C.P. 78290 San Luis Potosí, San Luis Potosí, Mexico |
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| 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. |
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| Keywords: | Gpn1 Gpn3 Gpn1&ndash Gpn3 interaction Gpn1&ndash Gpn3 nucleocytoplasmic shuttling Interdependent protein levels shRNA |
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