Peplowska Karolina, Markgraf Daniel F, Ostrowicz Clemens W, Bange Gert, Ungermann Christian
University of Osnabrück, Department of Biology, Biochemistry Section, Barbarastrasse 13, 49076 Osnabrück, Germany.
Dev Cell. 2007 May;12(5):739-50. doi: 10.1016/j.devcel.2007.03.006.
The dynamic equilibrium between vesicle fission and fusion at Golgi, endosome, and vacuole/lysosome is critical for the maintenance of organelle identity. It depends, among others, on Rab GTPases and tethering factors, whose function and regulation are still unclear. We now show that transport among Golgi, endosome, and vacuole is controlled by two homologous tethering complexes, the previously identified HOPS complex at the vacuole and a novel endosomal tethering (CORVET) complex, which interacts with the Rab GTPase Vps21. Both complexes share the four class C Vps proteins: Vps11, Vps16, Vps18, and Vps33. The HOPS complex, in addition, contains Vps41/Vam2 and Vam6, whereas the CORVET complex has the Vps41 homolog Vps8 and the (h)Vam6 homolog Vps3. Strikingly, the CORVET and HOPS complexes can interconvert; we identify two additional intermediate complexes, both consisting of the class C core bound to Vam6-Vps8 or Vps3-Vps41. Our data suggest that modular assembled tethering complexes define organelle biogenesis in the endocytic pathway.
高尔基体、内体以及液泡/溶酶体处囊泡裂变与融合之间的动态平衡对于维持细胞器特性至关重要。这尤其取决于Rab GTP酶和拴系因子，但其功能及调控仍不清楚。我们现在表明，高尔基体、内体和液泡之间的运输由两种同源拴系复合体控制，即先前在液泡中发现的HOPS复合体以及一种新的内体拴系（CORVET）复合体，它与Rab GTP酶Vps21相互作用。这两种复合体都共享四种C类Vps蛋白：Vps11、Vps16、Vps18和Vps33。此外，HOPS复合体还包含Vps41/Vam2和Vam6，而CORVET复合体含有Vps41的同源物Vps8和（h）Vam6的同源物Vps3。引人注目的是，CORVET和HOPS复合体可以相互转换；我们鉴定出另外两种中间复合体，二者均由与Vam6 - Vps8或Vps3 - Vps41结合的C类核心组成。我们的数据表明，模块化组装的拴系复合体定义了内吞途径中的细胞器生物发生。
