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Calmodulin inhibits the phosphorylation of spectrin in vitro.

Abstract：

:In vitro phosphorylation of purified spectrin dimer was studied in the presence of Ca2+-calmodulin (CaM). CaM inhibited autophosphorylation of the beta subunit of spectrin. The inhibitory effect (65% at a 32-fold molar excess) appeared to be due to a weak interaction of CaM with spectrin. CaM was similarly effective in a phosphatase-stimulated autothiophosphorylation of the beta subunit with [gamma-35S]ATP. Hence, its inhibitory effect was not due to stimulation of a spectrin-associated phosphatase activity. Phosphorylation of spectrin by the catalytic subunit of a cAMP-dependent protein kinase occurred in both subunits (1984, FEBS Lett. 169, 323). CaM selectively inhibited a cAMP-dependent phosphorylation of the alpha subunit of spectrin to 30% at two CaM per spectrin. It was ineffective on the cAMP-dependent phosphorylation of the beta subunit up to a 32-fold molar excess. These results yield functional evidence for a CaM-spectrin interaction. They further suggest that CaM can regulate the extent of a cAMP-dependent phosphorylation of the alpha subunit of spectrin.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Maretzki D,Lutz HU

doi

10.1016/0003-9861(86)90493-5

subject

Has Abstract

pub_date

1986-04-01 00:00:00

pages

469-77

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(86)90493-5

journal_volume

246

pub_type

杂志文章

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