Modification of calmodulin function by enzymatic carboxyl methylation

Gagnon, Claude; Kelly, Susan J.; Manganiello, Vincent C.; Vaughan, Martha; Odya, Charles E.; Strittmatter, Warren J.; Hoffman, Andrew R.; Hirata, Fusao

doi:10.1038/291515a0

Cited by 102 publications

(45 citation statements)

References 18 publications

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“…As we have shown, there was no observable change in the electrophoretic mobility of PCaM in the presence or absence of Ca2+, suggesting that phosphorylation of CaM may suppress its interaction with Ca2 . Similarly, it has been shown that methylation of CaM is also followed by an insensitivity to Ca2' (13). Some Ca2+-independent properties of CaM have already been reported as, for example, the Ca2+-independent stimulation ofBordetella pertussis adenylate cyclase by CaM (15 (21).…”

Section: Methodsmentioning

confidence: 98%

Evidence for a phosphorylated form of calmodulin in chicken brain and muscle.

Plancke¹,

Lazarides²

1983

Mol. Cell. Biol.

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Phosphocalmodulin (PCaM) was identified after analysis of calmodulin (CaM) preparations by two-dimensional gel electrophoresis by using a modified ampholyte system to resolve very acidic proteins. The analysis of CaM prepared by the conventional procedure based upon its heat resistance and acidity as well as the analysis of whole urea extracts from brain showed that PCaM was a major component in this tissue. PCaM was 1 pH unit more acidic than CaM, and its electrophoretic mobility, unlike CaM, was not changed by either calcium or ethylene glycol-bis(beta-aminoethyl ether)-N,N-tetraacetic acid. In urea extracts of brain prepared in buffers containing phosphate and sodium fluoride, PCaM was as prominent as CaM; it was partially converted into CaM after elution from the gel and reelectrophoresis. Amino acid analysis of PCaM and CaM purified by two-dimensional gel electrophoresis showed the same composition for the two proteins, including their trimethyllysine content. Incorporation of 32P occurred exclusively into the acidic variant when brain slices were incubated with H332PO4; amino acid analysis showed that the phosphate was bound to serine residues. CaM was found also to be phosphorylated in vitro by a phosphorylase kinase preparation from skeletal muscle.

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Section: Methodsmentioning

confidence: 98%

Evidence for a phosphorylated form of calmodulin in chicken brain and muscle.

Plancke¹,

Lazarides²

1983

Mol. Cell. Biol.

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“…5). Gagnon et al (20) reported that calmodulin is a good substrate for protein carboxyl methyltransf erase and that methylated cal modulin inhibits the stimulatory effect of calmodulin on cyclic nucleotide phosphodies terase. In the same manner, if methylated calmodulin attenuates the effect of cal modulin on the contractile response of smooth muscle, superprecipitation of uterine myosin B should be affected by L-methionine, SAM and blockers of SAM-dependent transmethylation.…”

Section: Discussionmentioning

confidence: 99%

General characteristics of the superprecipitation reaction of rat crude uterine myosin B: Effects of L-methionine and/or transmethylation blockers on the reaction.

et al. 1987

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Abstract-The characteristics of superprecipitation of uterine myosin B from 170-estradiol-3-benzoate-treated rats and the effects of L-methionine and/or 3-deazaadenosine (3-DAA) plus homocysteine thiolactone (HCTL) on the reaction were investigated. The slope and plateau phases of the superprecipitation were dependent on ATP, calcium and magnesium. The calmodulin antagonists, tri fluoperazine and N-(6-aminohexyl)-5-chloro-1-naphthalene sulfonamide, inhib

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“…For this reason it seemed very important when it was reported [5] that the regulatory protein calmodulin could be carboxylmethylated not only in vitro but also in living cells. Walker ascites carcinoma cells were incubated with L-[methyl-3H]-methionine, purified calmodulin by affinity chromatography, and found that also under these conditions calmodulin contained carboxylmethyl esters.…”

Section: Introductionmentioning

confidence: 99%