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

Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56(lck).

Molecular biology of the cell - 1 May 2000

Bijlmakers M J, Marsh M

Abstract excerpt

Tyrosine kinases of the Src family are synthesized as cytosolic proteins that subsequently translocate to membranes. Little is known of the mechanisms responsible for targeting these proteins to membranes, although a role for the cytosolic chaperone Hsp90 has been proposed. Here, we have studied the involvement of Hsp90 in the synthesis, membrane binding, and maintenance of the Src-kinase Lck. Using specific...

Read the complete abstract on PubMed

Topics

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

Share to Benzoquinones
Share to HSP90 Heat-Shock Proteins
Share to Lactams, Macrocyclic

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

Share to Lactones

Share to Lymphocyte Specific Protein Tyrosine Kinase p56(lck)

Share to Macrolides

Share to Quinones

Share to src-Family Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 10793137
DOI: 10.1091/mbc.11.5.1585
PMCID: PMC14869

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

Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56(lck).PMID 10793137Read ↗

Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90.Semantic proximity Read ↗

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

Rapid plasma membrane anchoring of newly synthesized p59fyn: selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3.Semantic proximity Read ↗

Dynamic palmitoylation of lymphoma proprotein convertase prolongs its half-life, but is not essential for trans-Golgi network localization.Semantic proximity Read ↗

Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation.Semantic proximity Read ↗

Mutants of the protein serine kinase PSKH1 disassemble the Golgi apparatus.Semantic proximity Read ↗

Plasma membrane localization of the Yck2p yeast casein kinase 1 isoform requires the C-terminal extension and secretory pathway function.Semantic proximity Read ↗

Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.Semantic proximity Read ↗

Role of the cytosolic chaperones Hsp70 and Hsp90 in maturation of the cardiac potassium channel HERG.Semantic proximity Read ↗

Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation.Semantic proximity Read ↗

Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase.Semantic proximity Read ↗

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