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

Functional analysis of the SH2 and SH3 domains of the lck tyrosine protein kinase.

Oncogene - 1 Oct 1992

Reynolds P J, Hurley T R, Sefton B M

Abstract excerpt

p56lck is a lymphoid cell-specific member of the src family of cytoplasmic tyrosine kinases. In helper and cytotoxic T cells it is physically associated with the CD4 and CD8 surface antigens and appears to play a role in signal transduction during T-cell activation. p56lck contains both an SH3 and an SH2 Src homology domain. Such domains have been suggested to play a role in the regulation of the activity or...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cell Transformation, Neoplastic
Share to Molecular Sequence Data

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

Share to Mutation

Share to Phosphorylation

Share to Proto-Oncogene Proteins

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 1408136

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

Functional analysis of the SH2 and SH3 domains of the lck tyrosine protein kinase.PMID 1408136Read ↗

The SH2 domain is required for stable phosphorylation of p56lck at tyrosine 505, the negative regulatory site.Semantic proximity Read ↗

Generation and characterization of transforming variants of the lck tyrosine protein kinase.Semantic proximity Read ↗

Role of the autophosphorylation site on the biological function of pp56lck.Semantic proximity Read ↗

Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation.Semantic proximity Read ↗

Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck.Semantic proximity Read ↗

SH3 domains specifically regulate kinase activity of expressed Src family proteins.Semantic proximity Read ↗

Expression of the T-Cell–Specific Tyrosine Kinase Lck in Normal B-1 Cells and in Chronic Lymphocytic Leukemia B CellsSemantic proximity Read ↗

Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src.Semantic proximity Read ↗

Association of p56lck with IL-2 receptor beta chain is critical for the IL-2-induced activation of p56lck.Semantic proximity Read ↗

The role of competing mechanisms on Lck regulation.Semantic proximity Read ↗

The unique amino-terminal domain of p56lck regulates interactions with tyrosine protein phosphatases in T lymphocytes.Semantic proximity Read ↗

<i>In Vivo</i>Consequences of Disrupting SH3-Mediated Interactions of the Inducible T-Cell KinaseSemantic proximity Read ↗

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