Emerging New Roles of GM130, a cis-Golgi Matrix Protein, in Higher Order Cell Functions

Abstract

Abstract. GM130 is a peripheral membrane protein strongly attached to the Golgi membrane and is isolated from the detergent and salt resistant Golgi matrix. GM130 is rich in coiled-coil structures and predicted to take a rod-like shape. Together with p115, giantin, and GRASP65, GM130 facilitates vesicle fusion to the Golgi membrane as a vesicle "tethering factor". GM130 is also involved in the maintenance of the Golgi structure and plays a major role in the disassembly and reassembly of the Golgi apparatus during mitosis. Emerging evidence suggests that GM130 is involved in the control of glycosylation, cell cycle progression, and higher order cell functions such as cell polarization and directed cell migration. This creates the potential for novel Golgitargeted drugs and treatments for various diseases including glycosylation defects, immune diseases, and cancer.

Spemann organizer gene Goosecoid promotes delamination of neuroblasts from the otic vesicle

“…1S). Because Gsc is known to regulate EMT (22,28), we also examined expression of GM130, a Golgi marker that undergoes a dramatic basal relocalization as cells undergo EMT (30,31). The pattern of GM130 staining in the otic floor revealed that the highest rate of EMT occurs in the region where ngn1 and gsc are coexpressed (Fig.…”

TFE3, HSP47, and CREB3 Pathways of the Mammalian Golgi Stress Response

“…Of note, the expression of GCP60 is markedly elevated in the striatum of Huntington disease (HD) patients, and enhanced levels of GCP60 elicited by endoplasmic reticulum, mitochondrial, and Golgi stresses may account for HD-associated neurodegeneration (Greninger et al, 2013). GM130 (also called Golgin-95) and Golgin-160 are cis-Golgi-localized members of Golgi family of coiled-coil tethering proteins and play important roles in the stacking of Golgi cisternae and in vesicular transport as a vesicle tethering factor (Nakamura, 2010). Giantin is a Golgi rim-localized member of the Golgin family and plays a role in vesicle tethering in conjunction with GM130 (Witkos and Lowe, 2015).…”

GM130, a cis-Golgi protein, regulates meiotic spindle assembly and asymmetric division in mouse oocyte

“…1 Together with its interacting partner proteins, including P115, giantin, GRASP65 and Rab GTPases, GM130 is involved in the regulation of ER-to-Golgi transport, glycosylation and maintenance of Golgi structure. 2 Recently, increasing evidence has indicated that GM130 has unexpected roles in the control of cell polarization, migration and division. [3][4][5][6][7] Golgi-nucleated microtubules, which were first identified by in vitro studies, 8 are preferentially oriented toward the leading edge of a motile cell and are necessary for directional protein transport.…”