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. 2019 Jul 30;16(5):862–877. doi: 10.1080/15548627.2019.1643656

Figure 9.

Figure 9.

Function of MtCAS31 in MtPIP2;7 autophagic degradation. (A) Detection of the MtATG8a-MtCAS31-MtPIP2;7 interaction by coimmunoprecipitation. Total proteins were extracted from the roots of transgenic M. truncatula, which express MtCAS31-FLAG. Medtr6g012980-FLAG was employed as the negative control. Total proteins were incubated with anti-FLAG beads to immunoprecipitate the target protein. Coprecipitated proteins were analyzed by immunoblotting using anti-ATG8 and anti-MtPIP2;7. (B) In the absence of stress, MtPIP2;7 is localized to the PM to transport water from soil into plant cells. Under drought stress, MtCAS31 is highly induced and participates in protein quality control. MtCAS31 works as a cargo receptor to form the MtPIP2;7-MtCAS31-MtATG8 complex, which promotes MtPIP2;7 autophagic degradation and thus reduces water loss. MtCAS31 may facilitate the autophagic degradation of other proteins, which needs to be examined in further studies.