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9.B.392.  The Golgi Apparatus Golgin (Golgin) Family

These proteins are involved in maintaining the Golgi structure, stimulating the formation of Golgi stacks and ribbons (Diao et al. 2003), and in intra-Golgi retrograde transport. Coiled-coil proteins of the golgin family have been implicated in intra-Golgi transport through tethering coat protein complex I (COPI) vesicles. The p115-golgin tether is the best studied. Malsam et al. 2005 characterized the golgin-84-CASP tether. The vesicles bound by this tether were strikingly different from those bound by the p115-golgin tether in that they lacked members of the p24 family of putative cargo receptors and contained enzymes instead of anterograde cargo. Microinjected golgin-84 or CASP inhibited Golgi-enzyme transport to the endoplasmic reticulum, further implicating this tether in retrograde transport. These and other golgins may modulate the flow patterns within the Golgi stack (Malsam et al. 2005).

The plant Golgi apparatus is responsible for the processing of proteins received from the ER, and their distribution to multiple destinations within the cell. Golgi matrix components, such as golgins, are tethering factors that mediate the physical connections between Golgi bodies and the ER. Golgins are  anchored to the Golgi membrane by the C-terminus either throughTMSs or interaction with small regulatory GTPases. The golgin N-terminus contains long coiled-coil domains which consist of a number of alpha-helices wrapped around each other to form a structure similar to a rope being made from several strands, reaching into the cytoplasm. In animal cells golgins are implicated in specific recognition of cargo. The plant golgin Atgolgin-84A is a tethering factor at the ER-Golgi interface.  Without it, transport between the ER and Golgi bodies is impaired, and cargo proteins are redirected to the vacuole (Vieira et al. 2020). Both O- and N-glycans appear to function as generic Golgi export signals at the trans-Golgi to promote exocytic trafficking (Sun et al. 2020).


References associated with 9.B.392 family:

Cao, H., X. Li, Z. Wang, M. Ding, Y. Sun, F. Dong, F. Chen, L. Liu, J. Doughty, Y. Li, and Y.X. Liu. (2015). Histone H2B Monoubiquitination Mediated by HISTONE MONOUBIQUITINATION1 and HISTONE MONOUBIQUITINATION2 Is Involved in Anther Development by Regulating Tapetum Degradation-Related Genes in Rice. Plant Physiol. 168: 1389-1405. 26143250
Diao, A., D. Rahman, D.J. Pappin, J. Lucocq, and M. Lowe. (2003). The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation. J. Cell Biol. 160: 201-212. 12538640
Du, Y., W. He, C. Deng, X. Chen, L. Gou, F. Zhu, W. Guo, J. Zhang, and T. Wang. (2016). Flowering-Related RING Protein 1 (FRRP1) Regulates Flowering Time and Yield Potential by Affecting Histone H2B Monoubiquitination in Rice (Oryza Sativa). PLoS One 11: e0150458. 26934377
Kim, J.H., S.D. Lim, K.H. Jung, and C.S. Jang. (2023). Overexpression of a C3HC4-type E3-ubiquitin ligase contributes to salinity tolerance by modulating Na homeostasis in rice. Physiol Plant 175: e14075. 38148225
Malsam, J., A. Satoh, L. Pelletier, and G. Warren. (2005). Golgin tethers define subpopulations of COPI vesicles. Science 307: 1095-1098. 15718469
Sun, X., H.C. Tie, B. Chen, and L. Lu. (2020). Glycans function as a Golgi export signal to promote the constitutive exocytic trafficking. J. Biol. Chem. 295: 14750-14762. 32826314
Vieira, V., C. Pain, S. Wojcik, T.S. Rossi, J. Denecke, A. Osterrieder, C. Hawes, and V. Kriechbaumer. (2020). Living on the edge: the role of Atgolgin-84A at the plant ER-Golgi interface. J Microsc. [Epub: Ahead of Print] 32700322