Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Zinc binding drives sheet formation by the SAM domain of diacylglycerol kinase δ.

Biochemistry - 9 Nov 2010

Knight Mary Jane, Joubert Marisa K, Plotkowski Megan L, Kropat Janette, Gingery Mari, Sakane Fumio, Merchant Sabeeha S, Bowie James U

Abstract excerpt

The diacylglycerol kinase (DGK) family of enzymes plays critical roles in lipid signaling pathways by converting diacylglycerol to phosphatidic acid, thereby downregulating signaling by the former and upregulating signaling by the latter second messenger. Ten DGK family isozymes have been identified to date, which possess different interaction motifs imparting distinct temporal and spatial control of DGK activity...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COS Cells

Share to Diacylglycerol Kinase

Share to Diglycerides

Share to Polymerization

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 20857926
DOI: 10.1021/bi101261x
PMCID: PMC3035719

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Zinc binding drives sheet formation by the SAM domain of diacylglycerol kinase δ.PMID 20857926Read ↗

An intact zinc finger motif of the C1B domain is critical for stability and activity of diacylglycerol kinase-ε.Semantic proximity Read ↗

Structural deficits in key domains of Shank2 lead to alterations in postsynaptic nanoclusters and to a neurodevelopmental disorder in humans.Semantic proximity Read ↗

A short linear motif, conserved from yeast to human, binds to members of the Spa2/GIT1 family of cortical scaffold proteinsSemantic proximity Read ↗

An architectural framework that may lie at the core of the postsynaptic density.Semantic proximity Read ↗

Shank3 Is Part of a Zinc-Sensitive Signaling System That Regulates Excitatory Synaptic Strength.Semantic proximity Read ↗

Regulation of lipid droplet turnover by ubiquitin ligases.Semantic proximity Read ↗

Palmitoyl Acyltransferase Activity of ZDHHC13 Regulates Skin Barrier Development Partly by Controlling PADi3 and TGM1 Protein Stability.Semantic proximity Read ↗

Lipid domain–dependent regulation of single-cell wound repairSemantic proximity Read ↗

A homologue of the human STRIPAK complex controls sexual development in fungiSemantic proximity Read ↗

Association of diacylglycerol kinase zeta with protein kinase C alpha: spatial regulation of diacylglycerol signaling.Semantic proximity Read ↗

Cryo-EM structure of the Hippo signaling integrator human STRIPAK.Semantic proximity Read ↗

Microtubule-dependent and independent roles of spastin in lipid droplet dispersion and biogenesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.