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. 2008 Oct;148(2):673-83.
doi: 10.1104/pp.108.124925.

Sorting and anterograde trafficking at the Golgi apparatus

Inhwan Hwang  1
Affiliations

Sorting and anterograde trafficking at the Golgi apparatus

Inhwan Hwang. Plant Physiol. 2008 Oct.
No abstract available

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Figures

Figure 1.
Figure 1.
A working model of the sorting of proteins destined for the central lytic vacuole and PSV from the Golgi apparatus and TGN. A, Sorting of proteins to the central lytic vacuole. Proteins containing the NPIR-type sorting motif are sorted by VSRs of the BP80 family. VSRs may interact with the adaptor proteins AP-1 and/or EpsinR1. AP-1 and EpsinR1 may interact with each other and with clathrin in the formation of CCVs. EpsinR1 interacts with AtVTI11 and actin filaments. This network of interactions between proteins may facilitate the formation of CCVs by efficiently recruiting accessory proteins to the TGN. In contrast, cargo receptors for proteins with CTPP or protein-specific sorting motifs are unknown. Furthermore, the adaptors of membrane proteins destined for the PVC and the lytic vacuole are largely unknown in plant cells. EpsinR2, which interacts with AtVTI12, AP-3, and clathrin, may also play a role in the trafficking of protein cargoes through CCVs. B, Sorting of proteins to the PSV. Proteins start to aggregate in the cis-Golgi and continue aggregating throughout the Golgi stacks until they bud off at the TGN as dense vesicles. RMR functions as a sorting receptor for the PSV. In the process of PSV protein aggregation through the Golgi stacks, it is not clear when RMR is involved in the recognition of PSV proteins. In addition, proteins may be sorted at the TGN to the PSV by the sorting receptor AtVSR1. AtVTI12 has been shown to play a role in the PSV pathway. However, it is not clear at present how it functions at the TGN. DV, Dense vesicle.
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