How VAMP72 evolved into VAMP727 through stepwise changes in plants (IMAGE)
Caption
This illustration shows how the membrane trafficking protein VAMP72 gradually changed during plant evolution to give rise to VAMP727, which functions in transporting storage proteins to vacuoles. The first step was the acquisition of a short insertion in its structure through alternative splicing. This insertion contained a non-canonical tyrosine-based motif, which enabled a partial shift in localization from the secretory to the vacuolar transport zone within the trans-Golgi network. Later, the insertion became more acidic and acquired a dileucine-like motif, enhancing its interaction with the AP-4 adaptor complex. These stepwise changes allowed VAMP72 to evolve into VAMP727, supporting the development of the efficient vacuolar transport system found in seed plants.
Credit
Takashi Ueda and Masaru Fujimoto
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