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Degradation-mediated protein quality control at the inner nuclear membrane

机译:内核膜降解介导的蛋白质质量控​​制

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摘要

An intricate machinery protects cells from the accumulation of misfolded, non-functional proteins and protein aggregates. Protein quality control pathways have been best described in the cytoplasm and the endoplasmic reticulum, however, recent findings indicate that the nucleus is also an important compartment for protein quality control. Several nuclear ubiquitinylation pathways target soluble and membrane proteins in the nucleus and mediate their degradation through nuclear proteasomes. In addition, emerging data suggest that nuclear envelope components are also degraded by autophagy, although the mechanisms by which cytoplasmic autophagy machineries get access to nuclear targets remain unclear. In this minireview we summarize the nuclear ubiquitin-proteasome pathways in yeast, focusing on pathways involved in the protein degradation at the inner nuclear membrane. In addition, we discuss potential mechanisms how nuclear targets at the nuclear envelope may be delivered to the cytoplasmic autophagy pathways in yeast and mammals.
机译:复杂的机制可保护细胞免受错误折叠的非功能性蛋白质和蛋白质聚集体的积累。蛋白质质量控​​制途径已经在细胞质和内质网中得到了最好的描述,但是,最近的发现表明细胞核也是蛋白质质量控​​制的重要组成部分。几种核泛素化途径靶向于细胞核中的可溶性和膜蛋白,并通过核蛋白酶体介导其降解。此外,新的数据表明,尽管细胞质自噬机制获得核靶标的机制尚不清楚,但核膜的成分也会被自噬降解。在这个小型回顾中,我们总结了酵母中的核泛素-蛋白酶体途径,重点研究了内核膜蛋白降解所涉及的途径。此外,我们讨论了潜在机制,如何将核膜上的核靶标传递到酵母和哺乳动物的细胞质自噬途径中。

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