Greg B. G. Moorhead
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View article: Lipidomic Profiling of Arabidopsis Chloroplast Protein Phosphatase Slp1 Mutants Reveals Altered Diurnal Lipid Remodeling
Lipidomic Profiling of Arabidopsis Chloroplast Protein Phosphatase Slp1 Mutants Reveals Altered Diurnal Lipid Remodeling Open
View article: Plant acetyl-CoA carboxylase: The homomeric form and the heteromeric form
Plant acetyl-CoA carboxylase: The homomeric form and the heteromeric form Open
View article: Phospho-proteomics identifies D-group MAP kinases as substrates of the Arabidopsis tyrosine phosphatase RLPH2
Phospho-proteomics identifies D-group MAP kinases as substrates of the Arabidopsis tyrosine phosphatase RLPH2 Open
Despite being one of the few bona fide plant tyrosine phosphatases, RLPH2 has no known substrates. Utilizing phospho-proteomics, we identified the activation loop phospho-tyrosine of several D-group mitogen activated protein kinases (MPKs)…
View article: Abstract 1639 Chloroplast protein phosphatase SLP1 counters protein kinase, casein kinase 2
Abstract 1639 Chloroplast protein phosphatase SLP1 counters protein kinase, casein kinase 2 Open
The serine/threonine protein phosphatase SLP1 is targeted to the higher plant chloroplast and has no known substrates. We have performed quantitative phosphoproteomics on wildtype, SLP1 knockout and over-expressor lines to uncover substrat…
View article: Abstract 2268 Protein phosphatase SLP1 is a novel regulator of chloroplastic metabolism
Abstract 2268 Protein phosphatase SLP1 is a novel regulator of chloroplastic metabolism Open
Photosynthesis is one of the most important biological phenomena on the planet. One regulatory mechanism for this process is the post-translational modification of proteins involved in catalyzing the light (in)dependent reactions occurring…
View article: Eukaryotic-like phosphoprotein phosphatase (PPP) enzyme evolution: interactions with environmental toxins and regulatory proteins
Eukaryotic-like phosphoprotein phosphatase (PPP) enzyme evolution: interactions with environmental toxins and regulatory proteins Open
Phosphoprotein phosphatases (PPPs) are a ubiquitous class of enzymes which dephosphorylate serine and threonine residues on substrate proteins involved in a wide variety of cellular processes. The active site of PPP enzymes are highly cons…
View article: Subcellular distribution of PP1 isoforms in holoenzyme complexes
Subcellular distribution of PP1 isoforms in holoenzyme complexes Open
Unlike its counterpart Ser/Thr kinases, the predominant Ser/Thr protein phosphatase 1 (PP1) is a promiscuous enzyme that gains its subcellular localization and substrate specificity from a large panel of regulatory proteins with which it a…
View article: Identification of Arabidopsis Protein Kinases That Harbor Functional Type 1 Peroxisomal Targeting Signals
Identification of Arabidopsis Protein Kinases That Harbor Functional Type 1 Peroxisomal Targeting Signals Open
Peroxisomes are eukaryotic specific organelles that perform diverse metabolic functions including fatty acid β-oxidation, reactive species metabolism, photorespiration, and responses to stress. However, the potential regulation of these fu…
View article: Affinity-based profiling of endogenous phosphoprotein phosphatases by mass spectrometry
Affinity-based profiling of endogenous phosphoprotein phosphatases by mass spectrometry Open
View article: The origin and radiation of the phosphoprotein phosphatase (PPP) enzymes of Eukaryotes
The origin and radiation of the phosphoprotein phosphatase (PPP) enzymes of Eukaryotes Open
View article: Origin of the Phosphoprotein Phosphatase (PPP) sequence family in Bacteria: Critical ancestral sequence changes, radiation patterns and substrate binding features
Origin of the Phosphoprotein Phosphatase (PPP) sequence family in Bacteria: Critical ancestral sequence changes, radiation patterns and substrate binding features Open
View article: LIKE SEX4 1 Acts as a β-Amylase-Binding Scaffold on Starch Granules during Starch Degradation
LIKE SEX4 1 Acts as a β-Amylase-Binding Scaffold on Starch Granules during Starch Degradation Open
In Arabidopsis (Arabidopsis thaliana) leaves, starch is synthesized during the day and degraded at night to fuel growth and metabolism. Starch is degraded primarily by β-amylases, liberating maltose, but this activity is preceded by…
View article: A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans
A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans Open
A "tug-of-war" between kinases and phosphatases establishes the phosphorylation states of proteins. While serine and threonine phosphorylation can be catalyzed by more than 400 protein kinases, the majority of serine and threonine dephosph…
View article: Crystal structures of the RLPH2 protein phosphatase from <i>Arabidopsis thaliana</i> reveal a novel mechanism for recognizing dually phosphorylated substrates
Crystal structures of the RLPH2 protein phosphatase from <i>Arabidopsis thaliana</i> reveal a novel mechanism for recognizing dually phosphorylated substrates Open
Despite belonging to the phosphoserine-and phosphothreonine-specific phosphoprotein phosphatase (PPP) family, Arabidopsis thaliana Rhizobiales-like phosphatase 2 (RLPH2) strongly prefers substrates bearing phosphorylated tyrosine residues.…
View article: Protein Kinases and Phosphatases of the Plastid and Their Potential Role in Starch Metabolism
Protein Kinases and Phosphatases of the Plastid and Their Potential Role in Starch Metabolism Open
Phospho-proteomic studies have confirmed that phosphorylation is a common mechanism to regulate protein function in the chloroplast, including the enzymes of starch metabolism. In addition to the photosynthetic machinery protein kinases (S…
View article: Aurora B opposes PP1 function in mitosis by phosphorylating the conserved PP1-binding RVxF motif in PP1 regulatory proteins
Aurora B opposes PP1 function in mitosis by phosphorylating the conserved PP1-binding RVxF motif in PP1 regulatory proteins Open
Phosphorylation within conserved motifs in regulatory subunits controls protein phosphatase 1 (PP1) holoenzyme assembly during mitosis.
View article: Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis
Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis Open
Histone deacetylases have central functions in regulating stress defenses and development in plants. However, the knowledge about the deacetylase functions is largely limited to histones, although these enzymes were found in diverse subcel…
View article: Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in <i>Arabidopsis</i>
Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in <i>Arabidopsis</i> Open
View article: AtSLP2 is an intronless protein phosphatase that co-expresses with intronless mitochondrial pentatricopeptide repeat (PPR) and tetratricopeptide (TPR) protein encoding genes
AtSLP2 is an intronless protein phosphatase that co-expresses with intronless mitochondrial pentatricopeptide repeat (PPR) and tetratricopeptide (TPR) protein encoding genes Open
Shewanella-like PPP family phosphatases (SLPs) are a unique lineage of eukaryote PPP-family phosphatases of bacterial origin which are not found in metazoans.1,2 Their absence in metazoans is marked by their ancient bacterial or…
View article: Recruitment of PP1 to the centrosomal scaffold protein CEP192
Recruitment of PP1 to the centrosomal scaffold protein CEP192 Open
View article: AtSLP2 is an intronless protein phosphatase that co-expresses with intronless mitochondrial pentatricopeptide repeat (PPR) and tetratricopeptide (TPR) protein encoding genes
AtSLP2 is an intronless protein phosphatase that co-expresses with intronless mitochondrial pentatricopeptide repeat (PPR) and tetratricopeptide (TPR) protein encoding genes Open
Shewanella-like PPP family phosphatases (SLPs) are a unique lineage of eukaryote PPP-family phosphatases of bacterial origin which are not found in metazoans.1,2 Their absence in metazoans is marked by their ancient bacterial or…
View article: Activation of Mitochondrial Protein Phosphatase SLP2 by MIA40 Regulates Seed Germination
Activation of Mitochondrial Protein Phosphatase SLP2 by MIA40 Regulates Seed Germination Open
Reversible protein phosphorylation catalyzed by protein kinases and phosphatases represents the most prolific and well-characterized posttranslational modification known. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) Shewane…
View article: Rhizobiales-like Phosphatase 2 from Arabidopsis thaliana Is a Novel Phospho-tyrosine-specific Phospho-protein Phosphatase (PPP) Family Protein Phosphatase
Rhizobiales-like Phosphatase 2 from Arabidopsis thaliana Is a Novel Phospho-tyrosine-specific Phospho-protein Phosphatase (PPP) Family Protein Phosphatase Open
View article: "PP2C7s", Genes Most Highly Elaborated in Photosynthetic Organisms, Reveal the Bacterial Origin and Stepwise Evolution of PPM/PP2C Protein Phosphatases
"PP2C7s", Genes Most Highly Elaborated in Photosynthetic Organisms, Reveal the Bacterial Origin and Stepwise Evolution of PPM/PP2C Protein Phosphatases Open
Mg+2/Mn+2-dependent type 2C protein phosphatases (PP2Cs) are ubiquitous in eukaryotes, mediating diverse cellular signaling processes through metal ion catalyzed dephosphorylation of target proteins. We have identified a distinct PP2C sequ…
View article: Actin dynamics tune the integrated stress response by regulating eukaryotic initiation factor 2α dephosphorylation
Actin dynamics tune the integrated stress response by regulating eukaryotic initiation factor 2α dephosphorylation Open
Four stress-sensing kinases phosphorylate the alpha subunit of eukaryotic translation initiation factor 2 (eIF2α) to activate the integrated stress response (ISR). In animals, the ISR is antagonised by selective eIF2α phosphatases comprisi…