An S-locus receptor-like kinase in plasma membrane interacts with calmodulin in Arabidopsis.
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 Ca(2+)-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.
Kim
Ho Soo
HS
Division of Applied Life Science, Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju, Republic of Korea.
Jung
Mi Soon
MS
Lee
Kyunghee
K
Kim
Kyung Eun
KE
Yoo
Jae Hyuk
JH
Kim
Min Chul
MC
Kim
Doh Hoon
DH
Cho
Moo Je
MJ
Chung
Woo Sik
WS
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology*; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary
D029681:Arabidopsis Proteins; D002147:Calmodulin; C538996:CBRLK1 protein, Arabidopsis; D017346:Protein Serine-Threonine Kinases