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

Phosphatidylinositol 4-phosphate 5-kinase α and Vav1 mutual cooperation in CD28-mediated actin remodeling and signaling functions.

Journal of immunology (Baltimore, Md. : 1950) - 1 Feb 2015

Muscolini Michela, Camperio Cristina, Porciello Nicla, Caristi Silvana, Capuano Cristina, Viola Antonella, Galandrini Ricciarda, Tuosto Loretta

Abstract excerpt

Phosphatidylinositol 4,5-biphosphate (PIP2) is a cell membrane phosphoinositide crucial for cell signaling and activation. Indeed, PIP2 is a pivotal source for second messenger generation and controlling the activity of several proteins regulating cytoskeleton reorganization. Despite its critical...

Read the complete abstract on PubMed

Topics

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

Share to Antigen-Presenting Cells
Share to CD28 Antigens

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Communication

Share to Oncogene Proteins

Share to Phosphotransferases (Alcohol Group Acceptor)

Share to Protein Interaction Domains and Motifs

Share to Proto-Oncogene Proteins c-vav

Share to T-Lymphocyte Subsets

Source

Identifiers

PMID: 25539813
DOI: 10.4049/jimmunol.1401643

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25539813-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphatidylinositol 4-phosphate 5-kinase α and Vav1 mutual cooperation in CD28-mediated actin remodeling and signaling functions.PMID 25539813Read ↗

Proline-serine-threonine phosphatase interacting protein 1 (PSTPIP1) controls immune synapse stability in human T cells.Semantic proximity Read ↗

Role of Phosphoinositides in Cellular Signaling, Functions and DiseasesSemantic proximity Read ↗

Cutting edge: CD28-mediated transcriptional and posttranscriptional regulation of IL-2 expression are controlled through different signaling pathways.Semantic proximity Read ↗

The N-terminal 20-amino acid region of guanine nucleotide exchange factor Vav1 plays a distinguished role in T cell receptor-mediated calcium signaling.Semantic proximity Read ↗

Lineage-specific requirement for the PH domain of Vav1 in the activation of CD4+ but not CD8+ T cells.Semantic proximity Read ↗

Vav1 oncogenic mutation inhibits T cell receptor-induced calcium mobilization through inhibition of phospholipase Cγ1 activation.Semantic proximity Read ↗

CD28 and Grb-2, relative to Gads or Grap, preferentially co-operate with Vav1 in the activation of NFAT/AP-1 transcriptionSemantic proximity Read ↗

ARPC5 Isoforms and Their Regulation by Calcium-Calmodulin-N-WASP Drive Distinct Arp2/3-dependent Actin Remodeling Events in CD4 T CellsSemantic proximity Read ↗

The scaffolding function of the RLTPR protein explains its essential role for CD28 co-stimulation in mouse and human T cells.Semantic proximity Read ↗

PAG orchestrates T cell immune synapse function by binding to actinSemantic proximity Read ↗

TAPP2 links phosphoinositide 3-kinase signaling to B-cell adhesion through interaction with the cytoskeletal protein utrophin: expression of a novel cell adhesion-promoting complex in B-cell leukemiaSemantic proximity Read ↗

Fyn-Binding Protein (Fyb)/Slp-76–Associated Protein (Slap), Ena/Vasodilator-Stimulated Phosphoprotein (Vasp) Proteins and the Arp2/3 Complex Link T Cell Receptor (Tcr) Signaling to the Actin CytoskeletonSemantic proximity Read ↗

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