Characterization of a protein serine kinase from yeast plasma membrane.

Kolarov, Jordan; Kulpa, Justyna; Baijot, M; Goffeau, André

doi:10.1016/s0021-9258(18)38015-3

Cited by 48 publications

(4 citation statements)

References 35 publications

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“…It is thus possible that lipid activation of the pump is indirect, mediated by stimulation of this kinase. Although we have no direct evidence that phosphorylation stimulates the plant proton pump, such evidence does exist in yeast (Kolarov et al, 1988;Chang & Slayman, 1991). The plant proton pump appears to be a substrate for a CDPK-like enzyme in vitro (M. R. Sussman, unpublished), but it remains to be established whether this occurs in vivo.…”

Section: Discussionmentioning

confidence: 84%

Calcium and lipid regulation of an Arabidopsis protein kinase expressed in Escherichia coli

Harper

Binder²,

Sussman³

1993

Biochemistry

118

117

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Calcium-dependent protein kinases (CDPKs) represent a new family of protein kinases which are proposed to contain, in a single polypeptide, both a kinase domain and an adjoining calmodulin-like domain with four calcium-binding EF-hand motifs [Harper, J.F., Sussman, M.R., Schaller, G.E., Putnam-Evans, C., Charbonneau, H., & Harmon, A.C. (1991) Science 252, 951-954]. DNA cloning and Western blot analysis indicate that multiple CDPK isoforms are present in the model plant system Arabidopsis thaliana. One CDPK gene called AK1 was isolated from Arabidopsis as a full-length cDNA. The predicted AK1 protein has a M(r) of 72,645 and is 116 amino acid residues longer at the amino terminus than the prototype CDPK alpha gene previously identified in soybean. The most highly conserved region between these two CDPKs is a region of 31 amino acids that joins the kinase and calmodulin-like domains. To verify the kinase activity of the enzyme encoded by AK1, a fusion of an amino-terminally truncated AK1 to the C-terminus of glutathione S-transferase was expressed in Escherichia coli. The fusion protein was purified and displayed a maximum kinase activity of 40 nmol of phosphate/(min.mg), using histone IIIs as a substrate. The enzyme activity was stimulated 3-6-fold by calcium and 2-5-fold by crude lipid. However, a synergistic stimulation of 16-30-fold was observed by the addition of both calcium and crude lipid. Lipid stimulation was specific for lysophosphatidylcholine and phosphatidylinositol and did not occur with the addition of phosphatidylserine or phosphatidylcholine.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionmentioning

confidence: 84%

Calcium and lipid regulation of an Arabidopsis protein kinase expressed in Escherichia coli

Harper

Binder²,

Sussman³

1993

Biochemistry

118

117

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“…Studies by Kolarov et al (1988) indicate that kinase-mediated phosphorylation of the yeast plasma membrane H+-ATPase stimulates activity. Whether phosphorylation modulates activity of the higher plant H+-ATPase in situ is as yet unknown but is an attractive hypothesis to explain rapid changes observed in electrophysiological measurements of plant cells after treatment with growth-regulating hormones and light.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a calcium- and lipid-dependent protein kinase associated with the plasma membrane of oat

Ge¹,

Ac²,

Mr³

1992

Biochemistry

126

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A protein kinase that is activated by calcium and lipid has been partially purified from the plasma membrane of oat roots. This protein kinase cross-reacts with four monoclonal antibodies directed against a soluble calcium-dependent protein kinase from soybean described previously [Putman-Evans, C. L., Harmon, A. C., & Cormier, M. J. (1990) Biochemistry 29, 2488-2495; Harper, J. F., Sussman, M. R., Schaller, G. E., Putnam-Evans, C., Charbonneau, H., & Harmon, A. C. (1991) Science 252, 951-954], indicating that the oat enzyme is a member of this calcium-dependent protein kinase family. Immunoblots demonstrate that the membrane-derived protein kinase is slightly larger than that observed in the cytosolic fraction of oat. Limited digestion of the membrane-derived kinase with trypsin generates a smaller water-soluble kinase that is still activated by calcium but is no longer activated by lipid. When posthomogenization proteolysis is minimized, the bulk of the immunoreactive kinase material is localized in the membrane. These results suggest that a calcium-dependent protein kinase observed in the supernatant fraction of oat extracts may originate in situ from a calcium- and lipid-dependent protein kinase which is associated with the oat plasma membrane. They further indicate that, in contrast to animal cells, the predominant calcium- and lipid-dependent protein kinase associated with the plasma membrane of plant cells has biochemical properties and amino acid sequence unlike protein kinase C.

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“…At present, the kinase(s) involved in ATPase phosphorylation are not clear. However, one likely candidate is a casein kinase associated with the yeast plasma membrane which has been shown to phosphorylate the ATPase on Ser residues in vitro (Kolarov et al ., 1988 ;Yanagita et al ., 1987) . Indeed, we have noted a number of consensus recognition sequences for casein kinase (Kemp and Pearson, 1990) distributed throughout the 100-kD polypeptide .…”

Section: Discussionmentioning

confidence: 99%

“…It has been suggested that the control of ATPase activity at the plasma membrane occurs via protein kinase-mediated phosphorylation. The ATPase is phosphorylated in vivo (McDonough and Mahler, 1982;Portillo and Mazon, 1985), and has been reported to serve as an in vitro substrate for a plasma membraneassociated casein kinase (Yanagita et al, 1987;Kolarov et al, 1988) . Furthermore, incubation ofpurified ATPase with acid phosphatase leads to a decrease in enzymatic activity (Kolarov et al, 1988) .…”

mentioning

confidence: 99%

Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport.

Chang

Slayman

1991

The Journal of Cell Biology

190

128

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. In this study we show that the plasma membrane [H+]ATPase of Saccharomyces cerevisiae is phosphorylated on multiple Ser and Thr residues in vivo. Phosphorylation occurs during the movement of newly synthesized ATPase from the ER to the cell surface, as revealed by the analysis of temperature-sensitive sec mutants blocked at successive steps of the secretory pathway. Two-dimensional phosphopeptide analysis of the ATPase indicates that, although most sites are phosphorylated at or before arrival in secretory vesi-T HE plasma membrane ATPase ofSaccharomyces cerevisiae is a proton pump that regulates cytoplasmic pH and provides the driving force for nutrient uptake (Serrano et al ., 1986, Serrano, 1989. Not surprisingly, in light of these critical physiologic functions, the [H+]ATPase is essential for cell viability. It has strong structural homology with other EX2 or P-type ATPases involved in maintaining ionic homeostasis, including the [Na+,K+] and Cat+ATPases of mammalian cells. Like other members of its class, the yeast ATPase has a catalytic subunit of -100 kD, hydrolyzes ATP via a transient aspartylphosphate intermediate, and is inhibited by low concentrations of vanadate. Sequence analysis of the PMAI gene encoding the yeast [H+]-ATPase predicts that the protein consists of a large central cytoplasmic domain containing putative sites for ATP binding and hydrolysis, anchored in the membrane by four hydrophobic segments at the NH2-terminal end and four to six hydrophobic segments at the COOH-terminal end .One approach taken in our laboratory to understanding structure-function relationships of the [H+]ATPase has been to study the acquisition of tertiary structure and activity during enzyme biogenesis . Recent work has established that newly synthesized [H+]ATPase becomes integrated into the endoplasmic reticulum membrane without cleavage of an NH2-terminal signal sequence, and is delivered to the cell surface via the secretory pathway (Holcomb et al., 1988) . In sec mutants blocked at discrete steps of the pathway, membrane biogenesis is prevented (Novick and Schekman, 1983 ;Tschopp et al ., 1984), and [H+]ATPase en route to the plasma membrane becomes trapped within the ER, Golgi compartment, or secretory vesicles (Brada and Schekman, 1988) . The ER and Golgi forms of the ATPase have not yet been examined for activity, but the enzyme accumulated in

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Characterization of a protein serine kinase from yeast plasma membrane.

Cited by 48 publications

References 35 publications

Calcium and lipid regulation of an Arabidopsis protein kinase expressed in Escherichia coli

Calcium and lipid regulation of an Arabidopsis protein kinase expressed in Escherichia coli

Characterization of a calcium- and lipid-dependent protein kinase associated with the plasma membrane of oat

Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport.

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