Samiksha Katiyar

Deciphering the unique autoregulatory mechanisms and substrate specificity of the understudied DCLK3 kinase linked to neurodegenerative diseases

Peng Zhao, Anup Kumar Prasad, Neha Gupta, Nathan Gravel et autres

Protein kinases represent one of the largest and most druggable protein families. Despite considerable progress in their understanding, approximately one-third of human kinases remain poorly characterized, known as the "dark" kinome. Doublecortin-like kinase 3 (DCLK3), a member of this elusive group, has …

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An atlas of bacterial serine-threonine kinases reveals functional diversity and key distinctions from eukaryotic kinases

Brady O’Boyle, Wayland Yeung, Samiksha Katiyar, Tomer M. Yaron et autres

Bacterial serine-threonine kinases (STKs) regulate diverse cellular processes associated with cell growth, virulence, and pathogenicity and are evolutionarily related to the druggable eukaryotic STKs. A deeper understanding of how bacterial STKs differ from their eukaryotic counterparts and how they have evolved to …

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Abstract 1645 Characterization of the dark kinase DCLK3 reveals isoform-specific modification and novel substrates

Jennifer Lu, Tej Shidhaye, Peng Zhao, Lance Wells et autres

HDAC, Histone deacetylase, Molecular dynamics, HDAC8 Metal-dependent lysine deacetylases (KDACs, also known as histone deacetylases or HDACs) are a family of enzymes responsible for reversing the post-translation modification of lysine acetylation.Because the eleven members of the KDAC family have a conserved catalytic …

Redox regulation and dynamic control of brain-selective kinases BRSK1/2 in the AMPK family through cysteine-based mechanisms

George N. Bendzunas, Dominic P. Byrne, Safal Shrestha, Leonard A. Daly et autres

In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications, including phosphorylation of Ser/Thr residues and oxidation of cysteine (Cys) residues. While regulation by activation segment phosphorylation of Ser/Thr residues is well understood, relatively little is known about …

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Author response: Redox regulation and dynamic control of brain-selective kinases BRSK1/2 in the AMPK family through cysteine-based mechanisms

George Bendzunas, Dominic P. Byrne, Safal Shrestha, Leonard A. Daly et autres

eLife assessmentThis study provides fundamental new knowledge into the role of reversible cysteine oxidation and reduction in protein kinase regulation.The data provide convincing evidence that intramolecular disulfide bonds serve a repressive regulatory role in the brain-selective kinases (BRSK) 1 and 2; part …

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Atlas of the Bacterial Serine-Threonine Kinases expands the functional diversity of the kinome

Brady O’Boyle, Wayland Yeung, Jing Lu, Samiksha Katiyar et autres

Abstract Bacterial serine-threonine protein kinases (STKs) regulate diverse cellular processes associated with cell growth, virulence, and pathogenicity. They are evolutionarily related to the druggable eukaryotic STKs. However, an incomplete knowledge of how bacterial STKs differ from their eukaryotic counterparts and how they …

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Multi-omics reveals new links between Fructosamine-3-Kinase (FN3K) and core metabolic pathways

Safal Shrestha, Rahil Taujale, Samiksha Katiyar, Natarajan Kannan

Fructosamine-3-kinases (FN3Ks) are a conserved family of repair enzymes that phosphorylate reactive sugars attached to lysine residues in peptides and proteins. Although FN3Ks are present across the Tree of Life and share detectable sequence similarity to eukaryotic protein kinases, the biological processes …

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Author response: Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms

George N. Bendzunas, Dominic P. Byrne, Safal Shrestha, Leonard A. Daly et autres

In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications (PTMs), including phosphorylation of Ser/Thr residues and oxidation of cysteine (Cys) residues. While regulation by activation segment phosphorylation of Ser/Thr residues is well understood, relatively little is known …

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Reviewer #1 (Public Review): Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms

George N. Bendzunas, Dominic P. Byrne, Safal Shrestha, Leonard A. Daly et autres

In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications (PTMs), including phosphorylation of Ser/Thr residues and oxidation of cysteine (Cys) residues. While regulation by activation segment phosphorylation of Ser/Thr residues is well understood, relatively little is known …

Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms

George N. Bendzunas, Dominic P. Byrne, Safal Shrestha, Leonard A. Daly et autres

Abstract In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications (PTMs), including phosphorylation of Ser/Thr residues and oxidation of cysteine (Cys) residues. While regulation by activation segment phosphorylation of Ser/Thr residues is well understood, relatively little is …

us, gb, jp (code pays fourni par la source)

Reviewer #1 (Public Review): Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms

George N. Bendzunas, Dominic P. Byrne, Safal Shrestha, Leonard A. Daly et autres

In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications (PTMs), including phosphorylation of Ser/Thr residues and oxidation of cysteine (Cys) residues. While regulation by activation segment phosphorylation of Ser/Thr residues is well understood, relatively little is known …

Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms

George N. Bendzunas, Dominic P. Byrne, Safal Shrestha, Leonard A. Daly et autres

Abstract In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications (PTMs), including phosphorylation of Ser/Thr residues and oxidation of cysteine (Cys) residues. While regulation by activation segment phosphorylation of Ser/Thr residues is well understood, relatively little is …

us, gb, jp (code pays fourni par la source)