InterPro domain: IPR039611

In general, Arabidopsis VQPs interacted specifically with the C-terminal WRKY domains of group I and the sole WRKY domains of group IIc WRKY transcription factors [ 1 , 2 ]. Arabidopsis VQPs reported to control stress responses include the calmodulin (CaM)-binding protein CamBP25 and VQ9, which regulate osmotic and salinity tolerance, respectively, the sigma factor binding proteins SIB1 and SIB2, which act as activators of WRKY33 in plant defence, and the negative regulator of the jasmonate defence pathway [ 3 ].

This entry includes a group of VQ motif-containing proteins (VQPs) from plants, including VQ4/11/13/19/31/33 from Arabidopsis. This subgroup of VQPs can be phosphorylated by the MAPKs MPK3 and MPK6, and have been named MPK3/6-targeted VQPs (MVQs). VQ4, also known as MVQ1, may act as an inhibitor of WRKY functions [ 4 ].

1. Structural and functional analysis of VQ motif-containing proteins in Arabidopsis as interacting proteins of WRKY transcription factors. Plant Physiol. 159, 810-25
2. The VQ Motif-Containing Protein Family of Plant-Specific Transcriptional Regulators. Plant Physiol. 169, 371-8
3. The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6 target a subclass of 'VQ-motif'-containing proteins to regulate immune responses. New Phytol. 203, 592-606