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

Internalization of the lymphocytic surface protein CD22 is controlled by a novel membrane proximal cytoplasmic motif.

The Journal of biological chemistry - 23 Oct 1998

Chan C H, Wang J, French R R, Glennie M J

Abstract excerpt

CD22 is a key receptor on B-lymphocytes that modulates signaling during antigenic stimulation. We have defined a novel cytoplasmic motif in human CD22 that controls its unusually rapid turnover at the plasma membrane. Chimeric and mutated CD22alpha cDNA vectors were constructed and stably transfected in CD22-negative Jurkat T-lymphocytic cells. Two assays were employed to measure CD22alpha internalization: first,...

Read the complete abstract on PubMed

Topics

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

Share to Antigens, CD
Share to Biological Transport
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Lymphocytes

Share to Mutation

Share to Protein Conformation

Share to Recombinant Fusion Proteins

Share to T-Lymphocytes

Source

Identifiers

PMID: 9774390
DOI: 10.1074/jbc.273.43.27809

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Internalization of the lymphocytic surface protein CD22 is controlled by a novel membrane proximal cytoplasmic motif.PMID 9774390Read ↗

CD22 ligand binding regulates normal and malignant B lymphocyte survival in vivo.Semantic proximity Read ↗

Distinct endocytic mechanisms of CD22 (Siglec-2) and Siglec-F reflect roles in cell signaling and innate immunity.Semantic proximity Read ↗

The transmembrane tyrosine of micro-heavy chain is required for BCR destabilization and entry of antigen into clathrin-coated vesicles.Semantic proximity Read ↗

CD22 regulates B cell receptor-mediated signals via two domains that independently recruit Grb2 and SHP-1.Semantic proximity Read ↗

The Ins and Outs of Antigen Uptake in B cellsSemantic proximity Read ↗

Anti-CD22–chimeric antigen receptors targeting B-cell precursor acute lymphoblastic leukemiaSemantic proximity Read ↗

Defining MacropinocytosisSemantic proximity Read ↗

Enterovirus A71 does not meet the uncoating receptor SCARB2 at the cell surfaceSemantic proximity Read ↗

CD22 EXON 12 deletion as a pathogenic mechanism of human B-precursor leukemiaSemantic proximity Read ↗

CD22 and Autoimmune DiseaseSemantic proximity Read ↗

Fc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization.Semantic proximity Read ↗

Genetic alteration of a bispecific ligand-directed toxin targeting human CD19 and CD22 receptors resulting in improved efficacy against systemic B cell malignancySemantic proximity Read ↗

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