Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus.

Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus.
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DOI:
10.1083/jcb.200108102
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发表时间:
2001-12-10
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Körner R
Körner R
中科院分区:
其他
文献类型:
--
作者:
Barr FA;Preisinger C;Kopajtich R;Körner R

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高尔基体是一种高度复杂的细胞器,由内质网到细胞表面的分泌途径上的一堆脑池膜组成。这种结构由外骨骼或高尔基体基质维持,外骨骼或高尔基体基质由卷曲螺旋蛋白家族、高尔金斯和其他外周膜成分(例如 GRASP55 和 GRASP65)构成。在这里,我们发现 TMP21、p24a 和 gp25L(p24 货物受体家族的成员)存在于体内与 GRASP55 和 GRASP65 的复合物中。 GRASP 直接与特定 p24 货物受体的细胞质结构域相互作用,具体取决于其寡聚状态,并且其中之一 p24a 的细胞质尾部 GRASP 结合位点的突变导致其被转运到细胞表面。这些结果表明,高尔基体基质的一项功能是帮助高尔基体中 p24 货物受体和其他膜蛋白的有效保留或隔离。
The Golgi apparatus is a highly complex organelle comprised of a stack of cisternal membranes on the secretory pathway from the ER to the cell surface. This structure is maintained by an exoskeleton or Golgi matrix constructed from a family of coiled-coil proteins, the golgins, and other peripheral membrane components such as GRASP55 and GRASP65. Here we find that TMP21, p24a, and gp25L, members of the p24 cargo receptor family, are present in complexes with GRASP55 and GRASP65 in vivo. GRASPs interact directly with the cytoplasmic domains of specific p24 cargo receptors depending on their oligomeric state, and mutation of the GRASP binding site in the cytoplasmic tail of one of these, p24a, results in it being transported to the cell surface. These results suggest that one function of the Golgi matrix is to aid efficient retention or sequestration of p24 cargo receptors and other membrane proteins in the Golgi apparatus.
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