GRASP depletion–mediated Golgi destruction decreases cell adhesion and migration via the reduction of a5ß1 integrin

Ahat, Erpan; Xiang, Yi; Zhang, Xiaoyan; Bekier, Michael E.; Wang, Yanzhuang

Proper glycosylation and sorting of proteins in the Golgi are required for many cell activities, such as cell attachment, migration, proliferation, and embryonic development (Zheng et al., 1994; Ono and Hakomori, 2004; Janik et al., 2010; Hang et al., 2017) . In addition, Golgi structural defects have been linked to human diseases, including Alzheimer's (Aridor and Balch, 1999; Joshi et al., 2014; Evin, 2015) , Huntington's (Hilditch-Maguire et al., 2000) , Parkinson's (Mizuno et al., 2001) , autoimmune diseases (Fritzler et al., 1984; Bizzaro et al., 1999) , cancer (Yoshimura et al., 1996; Roberts et al., 1998; Dennis et al., 1999; Diaz-Corrales et al., 2004; Krishnan et al., 2005) , viral infections (Ng et al., 2003) , and congenital disorders of glycosylation and Wiskott-Aldrich syndrome (Durand and Seta, 2000; Freeze and Ng, 2011) . However, the causal relationship between Golgi defects and disease pathogenesis remains largely unexplored. Therefore, it is crucial to understand how Golgi structure disruption affects essential cellular activities and physiology such as cell attachment, migration, and growth.