Promoting passage in plasmodesmata
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《细胞学杂志》
Lucas/AAAS
In plants, cell-to-cell communication is achieved through plasmodesmata, unique intercellular organelles that establish cytoplasmic and ER continuity between neighboring cells. Jung-Youn Lee, William Lucas (University of California, Davis, CA), and colleagues now identify a selective gatekeeper for this system, which they call NCAPP1.
Plasmodesmata are the conduits for many non–cell-autonomous proteins (NCAPs). Lee et al. figured that some NCAPs might bind to plasmodesmal proteins, so they used an affinity column based on an NCAP called CmPP16 and a cell wall fraction highly enriched for plasmodesmal proteins to identify NCAPP1.
As expected for a plasmodesmal function, colocalization of NCAPP1 and CmPP16 was observed at the ER near the orifice to plasmodesmata. A dominant–negative form of NCAPP1 altered trafficking of the NCAPs CmPP16, LEAFY, and the movement protein of Tobacco mosaic virus, but left trafficking of other NCAPs unaffected. Thus, NCAP movement is a regulated process, similar to nuclear pore trafficking. Lucas' group is now purifying other potential plasmodesmal proteins that traffic NCAPP1-independent cargos.
Reference:
Lee, J.-Y., et al. 2003. Science. 299:392–396.(When NCAPP1 (blue) is blocked (bottom), )
In plants, cell-to-cell communication is achieved through plasmodesmata, unique intercellular organelles that establish cytoplasmic and ER continuity between neighboring cells. Jung-Youn Lee, William Lucas (University of California, Davis, CA), and colleagues now identify a selective gatekeeper for this system, which they call NCAPP1.
Plasmodesmata are the conduits for many non–cell-autonomous proteins (NCAPs). Lee et al. figured that some NCAPs might bind to plasmodesmal proteins, so they used an affinity column based on an NCAP called CmPP16 and a cell wall fraction highly enriched for plasmodesmal proteins to identify NCAPP1.
As expected for a plasmodesmal function, colocalization of NCAPP1 and CmPP16 was observed at the ER near the orifice to plasmodesmata. A dominant–negative form of NCAPP1 altered trafficking of the NCAPs CmPP16, LEAFY, and the movement protein of Tobacco mosaic virus, but left trafficking of other NCAPs unaffected. Thus, NCAP movement is a regulated process, similar to nuclear pore trafficking. Lucas' group is now purifying other potential plasmodesmal proteins that traffic NCAPP1-independent cargos.
Reference:
Lee, J.-Y., et al. 2003. Science. 299:392–396.(When NCAPP1 (blue) is blocked (bottom), )