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These results suggest that RACK1A functions in rice innate immunity by interacting with multiple proteins in the OsRac1 immune complex.

We hypothesize that Tsp4 serves as a central organizing factor in MTJs by interacting with multiple ECM proteins, proteoglycans and receptors on muscle membranes.

Furthermore, recently, it has been demonstrated that RACK1 proteins are key regulators of innate immunity by interacting with multiple proteins in the Rac1 immune complex in rice [ 11].

MicroRNAs are small and non-coding RNA molecules that can regulate gene expression by interacting with multiple mRNAs and inducing either degradation of mRNA or inhibition of their translation to functional proteins [ 7, 14].

Activation of the FMS-like receptor tyrosine kinase 3 (FLT3), expressed on early multipotent hematopoietic cells, promotes cell survival and proliferation by interacting with multiple downstream targets including the AKT, STAT and MAP-kinase pathways.

Micro RNAs are small non-coding RNA molecules that can regulate gene expression by interacting with multiple mRNAs and inducing either translational suppression or degradation of mRNA.

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The PDZ domain is one of the most ubiquitous protein domains that is involved in coordinating signaling complex formation and protein networking by reversibly interacting with multiple binding partners.

These bacterial EPIYA effectors are delivered into host cells via type III or IV secretion, where they undergo tyrosine phosphorylation at the EPIYA motif and thereby manipulate host signalling by promiscuously interacting with multiple SH2 domain-containing proteins.

Insulin sensitivity is influenced by polygenic determinants interacting with multiple environmental factors.

Thus, the exploration of multiple genetic variations interacting with multiple environmental factors may be needed.

Previous studies have suggested that PTP-PEST suppresses triple-negative breast cancer cell transformation by interacting with and inhibiting multiple oncogenic tyrosine kinases, including EGFR and HER2 [66], [66].

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