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Biochem Biophys Res Commun. 2003 Jan 3;300(1):155-60.

Association of phospholamban with a cGMP kinase signaling complex.

Author information

1
Institut für Pharmakologie und Toxikologie, TU München, Biedersteiner Strasse 29, 80802 Munich, Germany. koller@ipt.med.tu-muenchen.de

Abstract

The cGMP kinase signaling complex identified previously in tracheal smooth muscle membranes contains a number of cGMP kinase substrates termed G0 through G4. G0, G1, and G2 were identified as IP(3) receptor I (IP(3)RI), IRAG, and cGMP kinase I. Sequencing of purified G3 and G4 showed that these proteins were proteolytic cleavage products of IRAG. However, the purified cGMP kinase signaling complex contained following additional proteins: alpha-actin, calponin H1, and phospholamban (PLB) as verified by MALDI-TOF as well as MS/MS sequencing and immune detection. The complex of these six proteins was immune precipitated by antibodies to each protein. The proteins were phosphorylated by the endogenous cGMP kinase I with the exception of alpha-actin and calponin H1. The complex did not contain the Ca(2+)-ATPase SERCA II. PLB, IP(3)RI, and cGMP kinase Ibeta were co-immune precipitated after expression in COS-7 cells. These results suggest that PLB may have additional functions to regulate the activity of SERCA II.

PMID:
12480535
[Indexed for MEDLINE]

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