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Proteome of ubiquitin/MVB pathway: possible involvement of iron-induced ubiquitylation of transferrin receptor in lysosomal degradation

机译：泛素/ MVB途径的蛋白质组：铁诱导的转铁蛋白受体泛素化可能参与溶酶体降解

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摘要

Ubiquitylation of membrane proteins triggers their endocytosis at the plasma membrane and subsequent lysosomal degradation through multivesicular bodies (MVBs). A dominant-negative mutant SKD1/Vps4B caused an accumulation of ubiquitylated membrane proteins in MVBs. We have identified 22 membrane proteins whose trafficking is potentially regulated by ubiquitylation. Nine of them, including transferrin receptor (TfR), are indeed ubiquitylated and/or accumulated in MVBs in the cells expressing mutant Vps4. While the recycling route and iron-regulated expression of TfR are well characterized, the mechanism by which the degradation of TfR is regulated is largely unknown. We show that an excess of iron enhances both TfR's ubiquitylation and degradation in lysosomes. Probably, the up-regulated expression of ferritin, an endogenous iron-chelating molecule, attenuated the iron-induced degradation of TfR. Exogenously introduced lysine-less TfR, compared to the wild-type one, showed resistance to the iron-induced ubiquitylation and degradation, when endogenous TfR, which most certainly heterodimerizes with exogenous ones, was depleted with siRNA. These data suggest that the iron-induced ubiquitylation and degradation of TfR along with MVB pathway physiologically plays an important role in iron homeostasis.
机译：膜蛋白的泛素化会触发它们在质膜的内吞作用，并随后通过多囊泡体（MVB）溶酶体降解。显性负突变SKD1 / Vps4B导致MVB中泛素化膜蛋白的积累。我们已经鉴定出22种膜蛋白，其运输可能受到泛素化的调节。它们中的九个，包括转铁蛋白受体（TfR），确实在表达突变型Vps4的细胞中被泛素化和/或积聚在MVB中。 TfR的回收途径和铁调节的表达已被很好地表征，但调节TfR降解的机制尚不清楚。我们表明，过量的铁会增强TfR的泛素化和溶酶体的降解。铁蛋白（一种内源性铁螯合分子）的表达上调可能减弱了铁诱导的TfR降解。与野生型相比，外源导入的无赖氨酸的TfR对铁诱导的泛素化和降解表现出抵抗力，而内源性TfR（肯定与外源性TfR异源二聚体）被siRNA耗尽。这些数据表明铁诱导的泛素化和TfR降解以及MVB途径在生理上对铁稳态起着重要作用。

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