School of Biomedical Sciences, Faculty of Medicine, The University of Queensland, Brisbane, QLD, 4072, Australia.
Cell Biol Int. 2019 Nov;43(11):1234-1244. doi: 10.1002/cbin.11118. Epub 2019 Jul 21.
GCC88 is a golgin coiled-coil protein at the trans-Golgi (TGN) that functions as a tethering factor for the endosome-derived retrograde transport vesicles. Here, we demonstrate that GCC88 is required for the endosome-to-TGN retrograde transport of the cation-independent mannose 6-phosphate receptor (CI-M6PR). The knockout of GCC88 perturbs the retrieval of CI-M6PR and decreases its cellular level at the steady state, which causes the improper processing of newly synthesized cathepsin-D, a lysosomal hydrolase dependent on CI-M6PR for its delivery to lysosomes. At the whole cell level, the knockout of GCC88 reduces the lysosomal proteolytic capacity but does not impair of the efficiency of autophagy within these cells.
GCC88 是一种位于反式高尔基体 (TGN) 的卷曲螺旋蛋白高尔基体衔接蛋白，作为内体衍生的逆行运输小泡的牵引因子发挥作用。在这里，我们证明 GCC88 是阳离子非依赖性甘露糖 6-磷酸受体 (CI-M6PR) 从内体到 TGN 的逆行运输所必需的。GCC88 的敲除扰乱了 CI-M6PR 的回收，并降低了其在稳定状态下的细胞水平，这导致新合成的组织蛋白酶 D 的处理不当，组织蛋白酶 D 是一种溶酶体水解酶，依赖于 CI-M6PR 将其递送至溶酶体。在细胞整体水平上，GCC88 的敲除降低了溶酶体的蛋白水解能力，但不损害这些细胞内自噬的效率。
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