Abstract:
:The inhibitory effect of actin on protein phosphorylation by three distinct protein kinases (CK-II, A-kinase and MAP-kinase) was examined in vitro. It was found that: (i) actin inhibits the activities of alpha-monomeric CK-II (CK-IIalpha) as well as oligomeric CK-II (alpha2beta2) in a dose-dependent manner, but has no effect on the activities of the two other kinases; and (ii) actin-induced inhibition of CK-II activity is due to the binding of actin to the alpha-subunit of CK-II and is non-competitive with its phosphate acceptors. In addition, it is demonstrated that actin binds directly to CK-II: both actin and CK-II are coprecipitated by anti-serum against Drosophila CK-IIbeta or by specific IgG against Ascaris suum muscle actin. The results presented here suggest that actin can suppress CK-II-mediated signal transduction.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Karino A,Tanoue S,Fukuda M,Nakamura T,Ohtsuki Kdoi
10.1016/s0014-5793(96)01266-5subject
Has Abstractpub_date
1996-12-02 00:00:00pages
317-21issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(96)01266-5journal_volume
398pub_type
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