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The Dictyostelium prestalk inducer differentiation-inducing factor-1 (DIF-1) triggers unexpectedly complex global phosphorylation changes.

Sugden C, Urbaniak MD, Araki T, Williams JG - Mol. Biol. Cell (2014)

Bottom Line: The results also provide evidence that the Ca(2+)/calmodulin-dependent phosphatase calcineurin plays a role in DIF-1 signaling to the DimB prestalk transcription factor.This accords with studies that suggest an antagonism between the two inducers and also with the rapid dephosphorylation of the cAMP receptor that we observe in response to DIF-1 and with the known inhibitory effect of DIF-1 on chemotaxis to cAMP.All MS data are available via ProteomeXchange with identifier PXD001555.

View Article: PubMed Central - PubMed

Affiliation: College of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.

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DIF-1–regulated phosphorylation sites in other cAMP-stimulated proteins. (A) Temporal profile for DIF-1–induced phosphorylation changes in class I sites on ElmoE (DDB0233920). (B) Heat-map representation of the temporal phosphorylation changes of class I DIF-1–regulated phosphorylation sites in myosin II components and regulators and other myosin heavy chains and their regulators. Averaged values, n ≥ 2. Asterisk indicates site previously identified as a cAMP-regulated phosphorylation site; dagger indicates TEDS site of phosphorylation on myosin I. (C) Temporal profile for class I DIF-1–induced phosphorylation changes to cAMP-regulated phosphorylation sites in myosin II components.
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Figure 8: DIF-1–regulated phosphorylation sites in other cAMP-stimulated proteins. (A) Temporal profile for DIF-1–induced phosphorylation changes in class I sites on ElmoE (DDB0233920). (B) Heat-map representation of the temporal phosphorylation changes of class I DIF-1–regulated phosphorylation sites in myosin II components and regulators and other myosin heavy chains and their regulators. Averaged values, n ≥ 2. Asterisk indicates site previously identified as a cAMP-regulated phosphorylation site; dagger indicates TEDS site of phosphorylation on myosin I. (C) Temporal profile for class I DIF-1–induced phosphorylation changes to cAMP-regulated phosphorylation sites in myosin II components.

Mentions: ElmoE is an essential component of the chemotaxis machinery and forms a direct link between cAMP-activated cAR1 and the actin cytoskeleton (Figure 4). It includes seven DIF-1–regulated class I sites. ElmoE is believed likely to exert its regulation by association with heterotrimeric G proteins and DOCK-like GEF proteins, regulating actin polymerization at the leading edge of migrating cells (Yan et al., 2012). All sites on ElmoE show consistent dephosphorylation in response to DIF-1 (Figure 8A).


The Dictyostelium prestalk inducer differentiation-inducing factor-1 (DIF-1) triggers unexpectedly complex global phosphorylation changes.

Sugden C, Urbaniak MD, Araki T, Williams JG - Mol. Biol. Cell (2014)

DIF-1–regulated phosphorylation sites in other cAMP-stimulated proteins. (A) Temporal profile for DIF-1–induced phosphorylation changes in class I sites on ElmoE (DDB0233920). (B) Heat-map representation of the temporal phosphorylation changes of class I DIF-1–regulated phosphorylation sites in myosin II components and regulators and other myosin heavy chains and their regulators. Averaged values, n ≥ 2. Asterisk indicates site previously identified as a cAMP-regulated phosphorylation site; dagger indicates TEDS site of phosphorylation on myosin I. (C) Temporal profile for class I DIF-1–induced phosphorylation changes to cAMP-regulated phosphorylation sites in myosin II components.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4325849&req=5

Figure 8: DIF-1–regulated phosphorylation sites in other cAMP-stimulated proteins. (A) Temporal profile for DIF-1–induced phosphorylation changes in class I sites on ElmoE (DDB0233920). (B) Heat-map representation of the temporal phosphorylation changes of class I DIF-1–regulated phosphorylation sites in myosin II components and regulators and other myosin heavy chains and their regulators. Averaged values, n ≥ 2. Asterisk indicates site previously identified as a cAMP-regulated phosphorylation site; dagger indicates TEDS site of phosphorylation on myosin I. (C) Temporal profile for class I DIF-1–induced phosphorylation changes to cAMP-regulated phosphorylation sites in myosin II components.
Mentions: ElmoE is an essential component of the chemotaxis machinery and forms a direct link between cAMP-activated cAR1 and the actin cytoskeleton (Figure 4). It includes seven DIF-1–regulated class I sites. ElmoE is believed likely to exert its regulation by association with heterotrimeric G proteins and DOCK-like GEF proteins, regulating actin polymerization at the leading edge of migrating cells (Yan et al., 2012). All sites on ElmoE show consistent dephosphorylation in response to DIF-1 (Figure 8A).

Bottom Line: The results also provide evidence that the Ca(2+)/calmodulin-dependent phosphatase calcineurin plays a role in DIF-1 signaling to the DimB prestalk transcription factor.This accords with studies that suggest an antagonism between the two inducers and also with the rapid dephosphorylation of the cAMP receptor that we observe in response to DIF-1 and with the known inhibitory effect of DIF-1 on chemotaxis to cAMP.All MS data are available via ProteomeXchange with identifier PXD001555.

View Article: PubMed Central - PubMed

Affiliation: College of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.

Show MeSH