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

An Autoinhibitory Role for the Pleckstrin Homology Domain of Interleukin-2-Inducible Tyrosine Kinase and Its Interplay with Canonical Phospholipid Recognition.

Biochemistry - 13 Jun 2017

Devkota Sujan, Joseph Raji E, Boyken Scott E, Fulton D Bruce, Andreotti Amy H

Abstract excerpt

Pleckstrin homology (PH) domains are well-known as phospholipid binding modules, yet evidence that PH domain function extends beyond lipid recognition is mounting. In this work, we characterize a protein binding function for the PH domain of interleukin-2-inducible tyrosine kinase (ITK), an immune cell specific signaling protein that belongs to the TEC family of nonreceptor tyrosine kinases. Its N-terminal PH...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Enzyme Stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipid Bilayers

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Phosphatidylinositol Phosphates

Share to Protein Interaction Domains and Motifs

Share to Protein Processing, Post-Translational

Share to Protein-Tyrosine Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 28516764
DOI: 10.1021/acs.biochem.6b01182
PMCID: PMC5956896

Genes

ITK
LCK
TEC

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An Autoinhibitory Role for the Pleckstrin Homology Domain of Interleukin-2-Inducible Tyrosine Kinase and Its Interplay with Canonical Phospholipid Recognition.PMID 28516764Read ↗

Rescue of the aggregation prone Itk Pleckstrin Homology domain by two mutations derived from the related kinases, Btk and Tec.Semantic proximity Read ↗

Phosphatidylserine binding is essential for plasma membrane recruitment and signaling function of 3-phosphoinositide-dependent kinase-1.Semantic proximity Read ↗

Biochemical and genetic analyses of the Tec kinases Itk and Rlk/Txk.Semantic proximity Read ↗

The C2 domain of Tollip, a Toll-like receptor signalling regulator, exhibits broad preference for phosphoinositides.Semantic proximity Read ↗

Substrate recognition of PLCγ1 via a specific docking surface on Itk.Semantic proximity Read ↗

IPMK: A versatile regulator of nuclear signaling events.Semantic proximity Read ↗

Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates.Semantic proximity Read ↗

T cell receptor (TCR) signaling in health and diseaseSemantic proximity Read ↗

Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX).Semantic proximity Read ↗

PHLPP1 Counter-regulates STAT1-mediated Inflammatory SignalingSemantic proximity Read ↗

LCK at the crossroad of immunodeficiency and autoimmunity: Mechanisms and therapeutic opportunities.Semantic proximity Read ↗

Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin.Semantic proximity Read ↗

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