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The new role of poly (rC)-binding proteins as iron transport chaperones: Proteins that could couple with inter-organelle interactions to safely traffic iron.
Biochimica et Biophysica Acta (BBA) - General Subjects ( IF 2.8 ) Pub Date : 2020-07-15 , DOI: 10.1016/j.bbagen.2020.129685
Izumi Yanatori 1 , Des R Richardson 2 , Shinya Toyokuni 1 , Fumio Kishi 3
Affiliation  

Background

Intracellular iron transport is mediated by iron chaperone proteins known as the poly(rC)-binding proteins (PCBPs), which were originally identified as RNA/DNA-binding molecules.

Scope of review

PCBPs assume a role as not only as cytosolic iron carriers, but also as regulators of iron transport and recycling. PCBP1 is involved in the iron storage pathway that involves ferritin, while PCBP2 is involved in processes that include: iron transfer from the iron importer, divalent metal ion transporter 1; iron export mediated by ferroportin-1; and heme degradation via heme oxygenase 1.

Major conclusions

Both PCBP1 and PCBP2 possess iron-binding activity and form hetero/homo dimer complexes. These iron chaperones have a subset of non-redundant functions and regulate iron metabolism independently.

General significance

This intracellular iron chaperone system mediated by PCBPs provide a transport “gateway” of ferrous iron that may potentially link with dynamic, inter-organelle interactions to safely traffic intracellular iron.



中文翻译:

聚(rC)结合蛋白作为铁转运伴侣的新作用:可以与细胞间相互作用相互作用的蛋白质,可以安全地转运铁。

背景

胞内铁转运是由称为聚(rC)结合蛋白(PCBP)的铁伴侣蛋白介导的,最初被鉴定为RNA / DNA结合分子。

审查范围

PCBP不仅扮演着胞质铁载体的角色,而且担当着铁运输和回收的调节者。PCBP1参与涉及铁蛋白的铁存储路径,而PCBP2涉及以下过程:从铁进口商的铁转移,二价金属离子转运蛋白1;Ferroportin-1介导的铁出口;并通过血红素加氧酶1降解血红素。

主要结论

PCBP1和PCBP2都具有铁结合活性,并形成杂/均二聚体。这些铁伴侣具有非冗余功能的子集,并独立调节铁代谢。

一般意义

由PCBP介导的这种细胞内铁分子伴侣系统提供了亚铁的运输“门户”,它可能潜在地与动态的,细胞间相互作用相互作用,从而安全地运输细胞内的铁。

更新日期:2020-08-11
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