Selected article for: "Golgi structure and protein synthesis"

Author: Ahat, Erpan; Xiang, Yi; Zhang, Xiaoyan; Bekier, Michael E.; Wang, Yanzhuang
Title: GRASP depletion–mediated Golgi destruction decreases cell adhesion and migration via the reduction of a5ß1 integrin
  • Document date: 2019_3_15
  • ID: rfs7m6or_27
    Snippet: In this study, we found that disruption of the Golgi structure by GRASP knockdown or knockout impacted multiple cell activities, including decreasing cell attachment, migration, and invasion, which could be explained by the decreased level of α5β1 integrin. We also found that GRASP depletion increased cell growth, which may be attributed to the increased overall protein synthesis and accelerated protein trafficking. Based on the literature, thi.....
    Document: In this study, we found that disruption of the Golgi structure by GRASP knockdown or knockout impacted multiple cell activities, including decreasing cell attachment, migration, and invasion, which could be explained by the decreased level of α5β1 integrin. We also found that GRASP depletion increased cell growth, which may be attributed to the increased overall protein synthesis and accelerated protein trafficking. Based on the literature, this is the first systematic study that links Golgi structure formation and function with cellular activities, including cell attachment, migration, and growth. It is reasonable to speculate that Golgi fragmentation found in diseases may cause global defects in protein trafficking, glycosylation, and secretion that impact essential cell activities. Thus, studying the cellular activities under Golgi destruction and discovering the factors that drive these changes will help us understand disease pathogenesis. In the long term, molecular tools may be developed to restore normal Golgi structure and function under disease conditions and thus to delay disease development.

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