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The translocation of effector proteins into the host plant cells is essential for pathogens to suppress plant immune responses. The oomycete pathogen Phytophthora infestans secretes AVR3a, a crucial virulence effector protein with an N-terminal RXLR motif that is required for this translocation. It has been reported that the RXLR motif of P. sojae Avr1b, which is a close homolog of AVR3a, is required for binding to phosphatidylinositol monophosphates (PIPs). However, in our previous report, AVR3a as well as Avr1b bind to PIPs not via RXLR but via lysine residues forming a positively-charged area in the effector domain. In this report, we examined whether other RXLR effectors whose structures have been determined bind to PIPs. Both P. capsici AVR3a11 and Hyaloperonospora arabidopsidis ATR1 have an RXLR motif in their N-terminal regions but did not bind to any PIPs. These results suggest that the RXLR motif is not sufficient for PIP binding.
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