Specificity of the cyclic GMP-bbmding activity and of a cyclic GMP-dependent cyclic GMP phosphodiesterase in Dictyostelium discoideum

Haastert, Peter J.M. van; Walsum, Hans van; Meer, Rob C. van der; Bulgakov, Roman; Konijn, Theo M.

doi:10.1016/0303-7207(82)90050-8

Cited by 26 publications

(28 citation statements)

References 30 publications

(21 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…cGMP-specific PDE was assayed following Van Haastert et al (43). Cells were starved in PBM at 1 ϫ 10 6 cells/ml for 6 h, collected by centrifugation, washed twice, resuspended in PB (3 mM Na 2 HPO 4 , 7 mM KH 2 PO 4 , pH 6.5) at 5 ϫ 10 7 cells/ml, and lysed through a 5-m filter.…”

Section: Methodsmentioning

confidence: 99%

A Cell Number-counting Factor Regulates Group Size inDictyostelium by Differentially Modulating cAMP-induced cAMP and cGMP Pulse Sizes

Tang¹,

Ammann²,

Gao³

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

A secreted counting factor (CF), regulates the size of Dictyostelium discoideum fruiting bodies in part by regulating cell-cell adhesion. Aggregation and the expression of adhesion molecules are mediated by relayed pulses of cAMP. Cells also respond to cAMP with a short cGMP pulse. We find that CF slowly down-regulates the cAMP-induced cGMP pulse by inhibiting guanylyl cyclase activity. A 1-min exposure of cells to purified CF increases the cAMP-induced cAMP pulse. CF does not affect the cAMP receptor or its interaction with its associated G proteins or the translocation of the cytosolic regulator of adenylyl cyclase to the membrane in response to cAMP. Pulsing streaming wild-type cells with a high concentration of cAMP results in the formation of small groups, whereas reducing cAMP pulse size with exogenous cAMP phosphodiesterase during stream formation causes cells to form large groups. Altering the extracellular cAMP pulse size does not phenocopy the effects of CF on the cAMP-induced cGMP pulse size or cell-cell adhesion, indicating that CF does not regulate cGMP pulses and adhesion via CF's effects on cAMP pulses. The results suggest that regulating cell-cell adhesion, the cGMP pulse size, or the cAMP pulse size can control group size and that CF regulates all three of these independently.

show abstract

Section: Methodsmentioning

confidence: 99%

A Cell Number-counting Factor Regulates Group Size inDictyostelium by Differentially Modulating cAMP-induced cAMP and cGMP Pulse Sizes

Tang¹,

Ammann²,

Gao³

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…The cytosolic fraction of Dictyostelium lysates contains a cGMP-binding protein with high affinity and specificity (22)(23)(24). The binding protein exists in two conformations, one with relatively low affinity and fast dissociation of the ligand (F-form) and the other with high affinity and slow dissociation (S-form); DNA promotes the conversion of the F-form to the S-form (25).…”

mentioning

confidence: 99%

Regulation of Guanylyl Cyclase by a cGMP-binding Protein during Chemotaxis in Dictyostelium discoideum

Kuwayama

Vanhaastert

1996

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Chemoattractants transiently activate guanylyl cyclase in Dictyostelium discoideum cells. Mutant analysis demonstrates that the produced cGMP plays an essential role in chemotactic signal transduction, controlling the actomyosin-dependent motive force. Guanylyl cyclase activity is associated with the particulate fraction of a cell homogenate. The addition of the cytosol stimulates guanylyl cyclase activity, whereas the cytosol plus ATP/Mg 2؉ inhibits enzyme activity. We have analyzed the regulation of guanylyl cyclase in chemotactic mutants and present evidence that a cGMP-binding protein mediates both stimulation and ATP-dependent inhibition of guanylyl cyclase.Upon chromatography of cytosolic proteins, cGMP binding activity co-elutes with both guanylyl cyclasestimulating and ATP-dependent-inhibiting activities. In addition, ATP-dependent inhibition of guanylyl cyclase activity is enhanced by the cGMP analogue 8-Br-cGMP, suggesting that a cGMP-binding protein regulates guanylyl cyclase activity. Mutant KI-4 has an aberrant cGMP binding activity with very low K d and shows a very small chemoattractant-mediated cGMP response; the cytosol from this mutant does not stimulate guanylyl cyclase. In contrast to KI-4, the aberrant cGMP binding activity of mutant KI-7 has a very high K d and chemoattractants induce a prolonged cGMP response. The cytosol of this mutant stimulates guanylyl cyclase activity, but ATP does not inhibit the enzyme. Thus, two previously isolated chemotactic mutants are defective in the activation and inhibition of guanylyl cyclase, respectively. The positive and negative regulation of guanylyl cyclase by its product cGMP may well explain how cells process the temporospatial information of chemotactic signals, which is necessary for sensing the direction of the chemoattractant.

show abstract

“…For stimulation of amoebae with K+, Na+, Mg2+ and Mn2+, the final ion concentration was 1.87 mM. Reactions were stopped by rapid addition of an equal volume of 3.5% perchloric acid, and cGMP assayed by radioimmunoassay as described in [23].…”

Section: Stimulation Of Amoebae and Cgmp Assaymentioning

confidence: 99%

Calcium induces cyclic GMP formation in Dictyostelium

Small¹,

Europe-Firmer²,

Newell³

1986

FEBS Letters

View full text Add to dashboard Cite

Cyclic GMP is rapidly formed a few seconds after binding of chemotactic signailing molecules to specific receptors on the cell surface of Dictyostelium amoebae. This phenomenon could be mimicked by addition of a pulse of Ca2+ to ~~eabili~d amoebae. The con~ntration of Ca 2+ for haIf-maximal response was 60 FM. Other ions (K+, Na+, Mg*+ or Mn2+) had no effect. A pulse of 5 PM IP, produced a cyclic GMP response of similar magnitude but IP, elicited no response. The data provide strong support for the hypothesis that cell surface receptor binding induces cyclic GMP formation by liberating Caz+ from internal stores.(Dictyostelium) cyclic GMP Chemotaxis Ca*+ INTRODUCTlONAmoebae of the cellular slime mould, Dictyostelium discoideum, respond chemotactically to signalling molecules such as folate during the foodseeking phase [l], and CAMP during the subsequent starvation phase [2] when they aggregate to form motile multicellular organisms [3]. These chemoattractants bind to separate cell surface receptors, yet appear to induce a group of internal responses common to both types of stimulus 141.Following a pulse of exogenous CAMP or folate, two of the initial responses identified are the polymerisation of actin associated with the cytoskeleton, peaking 3-5 s after stimulation (5lo], and the transient formation of cyclic GMP, which peaks 9-12 s after CAMP or folate binding , and is rapidly degraded by a specific cGMP phosphodiesterase [ 11,121. This cGMP formation has been implicated in chemotactic movement by studies which indicate its rapid accumulation following pulsing of several species of cellular slime mould (including D. ~is~~ide~rn, D. ~~~~e~rn~ and Po~ys~~o~dyfium violaceum) with their specific chemoattractants Abbreviations: IP,, inositol 1,4,5trisphosphate; IP2, inositol 1,4-bisphosphate [ 13,141. It is aIso strongly implicated in chemotaxis by the finding that streamer F mutants of D. discoideum (which lack the specific cCiMP phosphodiesterase and hence produce a large peak of cCMP in response to CAMP-receptor binding that persists for at least 1 min at elevated levels) show a chemotactic movement period that is greatly lengthened compared to the parental wild type f10, 15,16].Recently, studies in this laboratory have produced indirect evidence for the involvement of Ca'+ in chemotaxis in D. discoideum [17-191 and have revealed that IP3, when added to permeabilised amoebae, can mimic the action of chemoattractants on normal intact amoebae in inducing cGMP formation [ZO]. As IP3 in mammalian systems acts via release of intracellular Ca'+ 1211, it seemed worthwhile to study the direct effect of pulses of Ca2+ on the formation of cGMP in permeabilised amoebae. MATERIALS AND METHODS MaterialsIP3 (potassium salt) and IPz (potassium salt) were obtained from Amersham. Saponin and EGTA were obtained from Sigma.

show abstract

Specificity of the cyclic GMP-bbmding activity and of a cyclic GMP-dependent cyclic GMP phosphodiesterase in Dictyostelium discoideum

Cited by 26 publications

References 30 publications

A Cell Number-counting Factor Regulates Group Size inDictyostelium by Differentially Modulating cAMP-induced cAMP and cGMP Pulse Sizes

A Cell Number-counting Factor Regulates Group Size inDictyostelium by Differentially Modulating cAMP-induced cAMP and cGMP Pulse Sizes

Regulation of Guanylyl Cyclase by a cGMP-binding Protein during Chemotaxis in Dictyostelium discoideum

Calcium induces cyclic GMP formation in Dictyostelium

Contact Info

Product

Resources

About