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An S-locus receptor-like kinase in plasma membrane interacts with calmodulin in Arabidopsis
- Authors
- 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
- Issue Date
- 5-Jan-2009
- Publisher
- WILEY
- Keywords
- Calcium; Calmodulin; Calmodulin binding protein; Receptor-like kinase; Arabidopsis
- Citation
- FEBS LETTERS, v.583, no.1, pp 36 - 42
- Pages
- 7
- Indexed
- SCIE
SCOPUS
- Journal Title
- FEBS LETTERS
- Volume
- 583
- Number
- 1
- Start Page
- 36
- End Page
- 42
- ISSN
- 0014-5793
1873-3468
- 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.
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