[Effect of mutations imitating the phosphorylation by TRPM7 kinase on the function of the N-terminal domain of tropomodulin].
It has been shown that tropomodulin 1 is phosphorylated at serine and threonine residues by TRPM7 kinase. The phosphorylation sites for TRPM7 kinase in the N-terminal functional domain of tropomodulin 1 have been identified, which include tropomyosin-binding and actin-capping regions. It has been found that the phosphorylation-mimicking mutation T54E resulted in the loss of the capping ability of the N-terminal tropomodulin domain; however, its tropomyosin-binding ability did not change. We further hypothesize that the phosphorylation of tropomodulin by TRPM7 kinase may play a role in the regulation of the dynamics of actin filaments.
Dorovkov
M V
MV
Beznosov
S N
SN
Shah
S
S
Kotlianskaia
L
L
Kostiukova
A S
AS
D000199:Actins / Q000737:chemistry; D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D009154:Mutation; D010766:Phosphorylation; D020033:Protein Isoforms / Q000737:chemistry; D011494:Protein Kinases / Q000737:chemistry* / Q000235:genetics; D050051:Transient Receptor Potential Channels / Q000737:chemistry* / Q000235:genetics; D051348:Tropomodulin / Q000737:chemistry*
D000199:Actins; D020033:Protein Isoforms; D050051:Transient Receptor Potential Channels; D051348:Tropomodulin; D011494:Protein Kinases