Do Calcineurin B-Like Proteins Interact Independently of the Serine Threonine Kinase CIPK23 with the K+ Channel AKT1? Lessons Learned from a Ménage à Trois | Zendy

Christopher Grefen | Zendy; Michael R. Blatt | Zendy

Open Access

Do Calcineurin B-Like Proteins Interact Independently of the Serine Threonine Kinase CIPK23 with the K+ Channel AKT1? Lessons Learned from a Ménage à Trois

Author(s) -

Christopher Grefen,

Michael R. Blatt

Publication year - 2012

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.112.198051

Subject(s) - akt1 , threonine , dyrk1a , serine , calcineurin , akt2 , kinase , chemistry , biochemistry , microbiology and biotechnology , phosphorylation , biology , medicine , protein kinase b , transplantation

Calcineurin B-like proteins (CBLs) function as membrane-anchored Ca2+ sensors that, when activated, recruit a specific set of Ser-Thr kinases, calcineurin B-like protein-interacting protein kinases (CIPKs), to their sites of action (for review, see [Luan et al., 2009][1]; [Kudla et al., 2010][2]).

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