An S-locus receptor-like kinase in plasma membrane interacts with calmodulin in Arabidopsis

Abstract

Calmodulin-regulated protein phosphorylation plays a pivotal role in amplifying and diversifying the action of calcium ion. In this study, we identified a calmodulin-binding receptor-like protein kinase (CBRLK1) that was classified into an S-locus RLK family. The plasma membrane localization was determined by the localization of CBRLK1 tagged with a green fluorescence protein. Calmodulin bound specifically to a Ca2+-dependent calmodulin binding domain in the C-terminus of CBRLK1. The bacterially expressed CBRLK1 kinase domain could autophosphorylate and phosphorylates general kinase substrates, such as myelin basic proteins. The autophosphorylation sites of CBRLK1 were identified by mass spectrometric analysis of phosphopeptides. Structured summaryMINT-6800947:CBRLK1 (uniprotkb:Q9ZT06) and AtCaM2 (uniprotkb:P25069) bind (MI:0407) by electrophoretic mobility shift assay (MI:0413)MINT-6800966:AtCaM2 (uniprotkb:P25069) and CBRLK1 (uniprotkb:Q9ZT06) bind (MI:0407) by competition binding (MI:0405)MINT-6800930:CBRLK1 (uniprotkb:Q9ZT06) binds (MI:0407) to AtCaM2 (uniprotkb:P25069) by far Western blotting (MI:0047)MINT-6800978:AtCaM2 (uniprotkb:P25069) physically interacts (MI:0218) with CBRLK1 (uniprotkb:Q9ZT06) by cytoplasmic complementation assay (MI:0228)