Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic
Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic
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DOI：
10.1016/j.cell.2004.09.003
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发表时间：
2004-09-17
期刊：
影响因子：
64.5
通讯作者：
Helenius, A
中科院分区：
文献类型：
--
作者：
Pelkmans, L;Bürli, T;Helenius, A
内吞作用包括多种内化途径。一个突出的问题是小凹和内体途径是否相交。在活细胞中运输小凹蛋白 Caveolin-1 和两种货物复合物（猿猴病毒 40 和霍乱毒素）后，我们发现了一条 Rab5 依赖性途径，其中小凹囊泡靶向早期内体并形成独特且稳定的膜域。在内体中，低pH值选择性地使毒素从细胞膜穴结构域扩散到周围的膜中，而病毒仍然被困住。因此，我们得出的结论是，与囊泡运输中外壳蛋白的循环组装和解体不同，caveolin-1的寡聚复合物赋予小凹囊泡永久的结构稳定性，该小凹囊泡与内体短暂相互作用形成子结构域并通过区室特异性线索选择性地释放货物。
Endocytosis comprises several routes of internalization. An outstanding question is whether the caveolar and endosomal pathways intersect. Following transport of the caveolar protein Caveolin-1 and two cargo complexes, Simian Virus 40 and Cholera toxin, in live cells, we uncovered a Rab5-dependent pathway in which caveolar vesicles are targeted to early endosomes and form distinct and stable membrane domains. In endosomes, the low pH selectively allowed the toxin to diffuse out of the caveolar domains into the surrounding membrane, while the virus remained trapped. Thus, we conclude that, unlike cyclic assembly and disassembly of coat proteins in vesicular transport, oligomeric complexes of caveolin-1 confer permanent structural stability to caveolar vesicles that transiently interact with endosomes to form subdomains and release cargo selectively by compartment-specific cues.