Data di Pubblicazione:
2011
Citazione:
The p23 co-chaperone protein is a novel substrate of CK2 in Arabidopsis / K. Tosoni, A. Costa, S. Sarno, S. D’Alessandro, F. Sparla, L.A. Pinna, M. Zottini, M. Ruzzene. - In: MOLECULAR AND CELLULAR BIOCHEMISTRY. - ISSN 0300-8177. - 356:1-2(2011 Jun), pp. 245-254. ((Intervento presentato al 6. convegno International Conference on Protein Kinasc CK2/Symposium of the International Union of Biochemistry and Molecular Biology tenutosi a Cologne nel 2010 [10.1007/s11010-011-0969-0].
Abstract:
The ubiquitous Ser/Thr protein kinase CK2, which phosphorylates hundreds of substrates and is
essential for cell life, plays important roles also in plants; however, only few plant substrates have been identified so far. During a study aimed at identifying proteins targeted by CK2 in plant response to salicylic acid (SA), we found that the Arabidopsis co-chaperone protein p23 is a CK2
target, readily phosphorylated in vitro by human and maize CK2, being also a substrate for an endogenous casein kinase activity present in Arabidopsis extracts, which displays
distinctive characteristics of protein kinase CK2. We also demonstrated that p23 and the catalytic subunit of CK2 interact in vitro and possibly in Arabidopsis mesophyll protoplasts, where they colocalize in the cytosol and in the nucleus. Although its exact function is presently
unknown, p23 is considered a co-chaperone because of its ability to associate to the chaperone protein Hsp90; therefore, an involvement of p23 in plant signal transduction
pathways, such as SA signaling, is highly conceivable, and its phosphorylation may represent a fine mechanism for the regulation of cellular responses.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Arabidopsis; Casein kinase 2; Chaperone proteins; CK2; P23; Salicylic acid
Elenco autori:
K. Tosoni, A. Costa, S. Sarno, S. D’Alessandro, F. Sparla, L.A. Pinna, M. Zottini, M. Ruzzene
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