The J-domain protein Rme-8 interacts with Hsc70 to control clathrin-dependent endocytosis in Drosophila.
The J-domain protein Rme-8 interacts with Hsc70 to control clathrin-dependent endocytosis in Drosophila.
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DOI：
10.1083/jcb.200311084
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发表时间：
2004-03-29
期刊：
影响因子：
--
通讯作者：
Mellman I
中科院分区：
文献类型：
--
作者：
Chang HC;Hull M;Mellman I
通过筛选突变体表现出与显性负动力蛋白的相互作用，我们已经确定了受体介导的内吞作用（Rme）8，一个J-结构域的蛋白质先前被证明是必需的线虫内吞作用的果蝇同源。对果蝇Rme-8突变体的分析表明，Bride of sevenless的内化和示踪剂的摄取被阻断。此外，内体组织和网格蛋白的分布在Rme-8细胞中被极大地破坏，表明Rme-8参与网格蛋白依赖性过程。Rme-8突变体的表型与Hsc 70 -4的表型非常相似，表明这两个基因在共同的途径中起作用。事实上，生物化学和遗传数据表明，Rme-8通过其J结构域与Hsc 70 -4特异性相互作用。因此，Rme-8似乎作为一个意想不到的，但关键的共伴侣与Hsc 70的内吞作用。因为已知Hsc 70与另一种J蛋白生长素一起沿着在网格蛋白脱壳中起作用，所以其与Rme-8的相互作用表明Hsc 70可以与多种辅因子起作用，这可能解释了其在内吞途径上的多效性作用。
By screening for mutants exhibiting interactions with a dominant-negative dynamin, we have identified the Drosophila homologue of receptor-mediated endocytosis (Rme) 8, a J-domain–containing protein previously shown to be required for endocytosis in Caenorhabditis elegans. Analysis of Drosophila Rme-8 mutants showed that internalization of Bride of sevenless and the uptake of tracers were blocked. In addition, endosomal organization and the distribution of clathrin were greatly disrupted in Rme-8 cells, suggesting that Rme-8 participates in a clathrin-dependent process. The phenotypes of Rme-8 mutants bear a strong resemblance to those of Hsc70-4, suggesting that these two genes act in a common pathway. Indeed, biochemical and genetic data demonstrated that Rme-8 interacts specifically with Hsc70-4 via its J-domain. Thus, Rme-8 appears to function as an unexpected but critical cochaperone with Hsc70 in endocytosis. Because Hsc70 is known to act in clathrin uncoating along with auxilin, another J-protein, its interaction with Rme-8 indicates that Hsc70 can act with multiple cofactors, possibly explaining its pleiotropic effects on the endocytic pathway.
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