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

Kim, Ho Soo; Jung, Mi Soon; Lee, Kyunghee; Kim, Kyung Eun; Yoo, Jae Hyuk; Kim, Min Chul; Kim, Doh Hoon; Cho, Moo Je; Chung, Woo Sik

doi:10.1016/j.febslet.2008.11.046

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Volume 583, Issue 1 , Pages 36-42, 5 January 2009

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

Edited by Michael R. Sussman

Ho Soo Kim
- Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 900 Gajwa, Room No. 6-320, Jinju 660-701, Republic of Korea
- Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju 660-701, Republic of Korea
Mi Soon Jung
- Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 900 Gajwa, Room No. 6-320, Jinju 660-701, Republic of Korea
Kyunghee Lee
- Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 900 Gajwa, Room No. 6-320, Jinju 660-701, Republic of Korea
- Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju 660-701, Republic of Korea
Kyung Eun Kim
- Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 900 Gajwa, Room No. 6-320, Jinju 660-701, Republic of Korea
Jae Hyuk Yoo
- Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju 660-701, Republic of Korea
Min Chul Kim
- Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 900 Gajwa, Room No. 6-320, Jinju 660-701, Republic of Korea
Doh Hoon Kim
- Faculty of Plant Biotechnology, Dong-A University, Busan 604-714, Republic of Korea
Moo Je Cho
- Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 900 Gajwa, Room No. 6-320, Jinju 660-701, Republic of Korea
Woo Sik Chung
- Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 900 Gajwa, Room No. 6-320, Jinju 660-701, Republic of Korea
- Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju 660-701, Republic of Korea
- Corresponding author. Address: Division of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, 900 Gajwa, Room No. 6-320, Jinju 660-701, Republic of Korea. Fax: +82 55 759 9363.

Received 27 September 2008; received in revised form 28 October 2008; accepted 14 November 2008. published online 09 December 2008.

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 summary

MINT-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)

Abbreviations: AtCaM, Arabidopsis calmodulin, CaM, calmodulin, CaMBD, calmodulin binding domain, CaMBP, calmodulin binding protein, CBRLK1, calmodulin-binding receptor-like kinase, 5-FOA, 5-fluoroorotic acid, GST, glutathione S-transferase, HRP, horseradish peroxidase, N_ub and C_ub, N- and C-terminal halves of ubiquitin, respectively