Calmodulin and the cell cycle: Involvement in regulation of cell-cycle progression

Chafouleas, James G.; Bolton, Wade E.; Hidaka, Hiroyoshi; Boyd, A. E.; Means, Anthony R.

doi:10.1016/0092-8674(82)90373-7

Cited by 414 publications

(129 citation statements)

References 24 publications

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“…Assays were done in the presence of I mmol-1 -~ ethylene diaminetetraacetic acid (EDTA); the Ca z § concentrations used above represent the unchelated amount of Ca 2 § in the assay. Furthermore the calmodulin antagonist W-5, which causes 50% inhibition of calmodulin-dependent kinases when pres- Chafouleas et al 1982), had no effect on the GTP-dependent kinase at 2 mmol. l-1 final concentration.…”

Section: -1 In the Absence Of Mn 2 + Resulted In A Continualmentioning

confidence: 93%

A guanosine 5?-triphosphate-dependent protein kinase is localized in the outer envelope membrane of pea chloroplasts

Soll¹,

Fischer²,

Keegstra

1988

Planta

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Abstract.A guanosine 5'-triphosphate (GTP)-dependent protein kinase was detected in preparations of outer chloroplast envelope membranes of pea (Pisum sativum L.) chloroplasts. The proteinkinase activity was capable of phosphorylating several envelope-membrane proteins. The major phosphorylated products were 23-and 32.5-kilodalton proteins of the outer envelope membrane. Several other envelope proteins were labeled to a lesser extent. Following acid hydrolysis of the labeled proteins, most of the label was detected as phosphoserine with only minor amounts detected as phosphothreonine. Several criteria were used to distinguish the GTP-dependent protein kinase from an ATP-dependent kinase also present in the outer envelope membrane. The ATP-dependent kinase phosphorylated a very different set of envelope-membrane proteins. Heparin inhibited the GTP-dependent kinase but had little effect upon the ATP-dependent enzyme. The GTP-dependent enzyme accepted phosvitin as an external protein substrate whereas the ATP-dependent enzyme did not. The outer membrane of the chloroplast envelope also contained a phosphotransferase capable of transferring labeled phosphate from [7-32p]GTP to ADP to yield (7-32p]ATP. Consequently, addition of ADP to a GTP-dependent protein-kinase assay resulted in a switch in the pattern of labeled products from that seen with GTP to that typically seen with ATP.

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Section: -1 In the Absence Of Mn 2 + Resulted In A Continualmentioning

confidence: 93%

A guanosine 5?-triphosphate-dependent protein kinase is localized in the outer envelope membrane of pea chloroplasts

Soll¹,

Fischer²,

Keegstra

1988

Planta

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“…For example, 10 or 30 M W-7/W-13 reduces by ϳ15 or ϳ20 mV, respectively. W-12, which is about 10-fold less potent as a CaM inhibitor (47,48), decreases the magnitude of the zeta potential about 10-fold less effectively. Fig.…”

Section: Methodsmentioning

confidence: 99%

Membrane-permeable Calmodulin Inhibitors (e.g. W-7/W-13) Bind to Membranes, Changing the Electrostatic Surface Potential

Sengupta

Ruano

Tebar

et al. 2007

Journal of Biological Chemistry

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Membrane-permeable calmodulin inhibitors, such as the napthalenesulfonamide derivatives W-7/W-13, trifluoperazine, and calmidazolium, are used widely to investigate the role of calcium/calmodulin (Ca 2؉ /CaM) in living cells. If two chemically different inhibitors (e.g. W-7 and trifluoperazine) produce similar effects, investigators often assume the effects are due to CaM inhibition. Zeta potential measurements, however, show that these amphipathic weak bases bind to phospholipid vesicles at the same concentrations as they inhibit Ca 2؉ /CaM; this suggests that they also bind to the inner leaflet of the plasma membrane, reducing its negative electrostatic surface potential. This change will cause electrostatically bound clusters of basic residues on peripheral (e.g. Src and K-Ras4B) and integral (e.g. epidermal growth factor receptor (EGFR)) proteins to translocate from the membrane to the cytoplasm. We measured inhibitor-mediated translocation of a simple basic peptide corresponding to the calmodulin-binding juxtamembrane region of the EGFR on model membranes; W-7/W-13 causes translocation of this peptide from membrane to solution, suggesting that caution must be exercised when interpreting the results obtained with these inhibitors in living cells. We present evidence that they exert dual effects on autophosphorylation of EGFR; W-13 inhibits epidermal growth factordependent EGFR autophosphorylation under different experimental conditions, but in the absence of epidermal growth factor, W-13 stimulates autophosphorylation of the receptor in four different cell types. Our interpretation is that the former effect is due to W-13 inhibition of Ca 2؉

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“…This is supported by the observation that the calmodulin levels of the cdc mutants arrested at or before the G2 phase remained at low levels, but those of mutants arrested at the nuclear-division phase increase to the normal level. There are two controversial reports indicating that during the cell cycle in Chinese hamster ovary cells, the calmodulin level was minimum in the early G 1 phase and elevated twofold at either the early S phase (2) or the late G2 phase (12). When a calmodulin antagonist was added at the S phase, the cell cycle was blocked at the late G2 or early M phase (12).…”

Section: And Discussionmentioning

confidence: 99%

Cell cycle-dependent regulation of calmodulin levels in Saccharomyces cerevisiae.

Uno

Ohya

Anraku

et al. 1989

J. Gen. Appl. Microbiol.

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The calmodulin level in the cell division cycle yeast mutants defective at the G1 and S phases decreased to less than half of that in the wild type during incubation at high (37°C) temperature. The calmodulin levels were elevated twofold in parallel with the budding process during the cell cycle in wild-type cells. These levels decreased after cell duplication, and the G 1 daughter cells contained half the maximum calmodulin level found before cell duplication.Calmodulin is one of the intracellular calcium receptors responsible for regulating the function of various proteins. It exists in a wide variety of eukaryotes, and its structure and function are known to be highly conserved in those organisms examined (3, 7). Calmodulin from the yeast Saccharomyces cerevisiae was purified to complete homogeneity, and characterized under various criteria (10). The biochemical properties of the purified protein were similar to other calmodulins. The amino acid composition of yeast calmodulin was slightly different from the calmodulins from other sources. Recently the yeast calmodulin gene CMD1 was cloned and sequenced (4).The CMD1 gene is a unique, single-copy gene and its disruption results in a recessive-lethal mutation, indicating that calmodulin is essential for the growth of yeast cells (4). In mammalian cells, calmodulin levels are doubled at late Gl and early S phases (2) or at late G2 phase (12) during the cell cycle. This indicates the importance of calmodulin in the progression through the cell cycle.To investigate the function of calmodulin in the yeast cell cycle, we determined

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Calmodulin and the cell cycle: Involvement in regulation of cell-cycle progression

Cited by 414 publications

References 24 publications

A guanosine 5?-triphosphate-dependent protein kinase is localized in the outer envelope membrane of pea chloroplasts

A guanosine 5?-triphosphate-dependent protein kinase is localized in the outer envelope membrane of pea chloroplasts

Membrane-permeable Calmodulin Inhibitors (e.g. W-7/W-13) Bind to Membranes, Changing the Electrostatic Surface Potential

Cell cycle-dependent regulation of calmodulin levels in Saccharomyces cerevisiae.

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