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首页> 外文期刊>Cell metabolism >Molecular mechanism of hepcidin-mediated ferroportin internalization requires ferroportin lysines, not tyrosines or JAK-STAT
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Molecular mechanism of hepcidin-mediated ferroportin internalization requires ferroportin lysines, not tyrosines or JAK-STAT

机译：铁调素介导的铁转运蛋白内在化的分子机制需要铁转运蛋白赖氨酸而不是酪氨酸或JAK-STAT

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摘要

Ferroportin is the primary means of cellular iron efflux and a key component of iron metabolism. Hepcidin regulates Fpn activity by inducing its internalization and degradation. The mechanism of internalization is reported to require JAK2 activation, phosphorylation of Fpn tyrosine residues 302 and 303, and initiation of transcription through STAT3 phosphorylation. These findings suggest Fpn may be a target for therapeutic intervention through JAK2 modulation. To evaluate the proposed mechanism, Fpn internalization was assessed using several techniques combined with reagents that specifically recognized cell-surface Fpn. In vitro results demonstrated that Hepc-induced Fpn internalization did not require JAK2 or phosphorylation of Fpn residues 302 and 303, nor did it induce JAK-STAT signaling. In vivo, inhibition of JAK2 had no effect on Hepc-induced hypoferremia. However, internalization was delayed by mutation of two Fpn lysine residues that may be targets of ubiquitination.
机译：铁转运蛋白是细胞铁流出的主要手段，是铁代谢的关键组成部分。铁调素通过诱导其内在化和降解来调节Fpn活性。据报道，内在化的机制需要JAK2激活，Fpn酪氨酸残基302和303的磷酸化以及通过STAT3磷酸化的转录起始。这些发现表明，Fpn可能是通过JAK2调节进行治疗干预的靶标。为了评估提出的机制，使用几种技术结合特异性识别细胞表面Fpn的试剂评估了Fpn的内在化。体外结果表明，Hepc诱导的Fpn内在化不需要JAK2或Fpn残基302和303的磷酸化，也不诱导JAK-STAT信号传导。在体内，抑制JAK2对Hepc引起的低铁血症没有影响。但是，由于可能是泛素化的两个Fpn赖氨酸残基的突变而延迟了内部化。

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