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

Myristoylation cannot functionally replace the isoprenylation of Rab5.

Archives of biochemistry and biophysics - 10 Jan 1995

Li G, Barbieri M A, Stahl P D

Abstract excerpt

C-terminal isoprenylation is necessary for the small GTPase Rab5 to associate with early endosomes and to exert its regulatory function in endocytosis. In this study, we tested whether Rab5 could retain its membrane association and biological function if the isoprenylation were replaced by another type of lipid modification (myristoylation). Rab5 mutants were constructed that contained both isoprenylation and...

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 Biological Transport
Share to Biomarkers

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

Share to Cells, Cultured

Share to Cricetinae

Share to GTP-Binding Proteins

Share to Molecular Sequence Data

Share to Mutation

Source

Identifiers

PMID: 7840662
DOI: 10.1006/abbi.1995.1070

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

Myristoylation cannot functionally replace the isoprenylation of Rab5.PMID 7840662Read ↗

The role of the hypervariable C-terminal domain in Rab GTPases membrane targeting.Semantic proximity Read ↗

Membrane targeting of Rab GTPases is influenced by the prenylation motif.Semantic proximity Read ↗

Myristoylation is required for the intracellular localization and endocytic function of ARF6.Semantic proximity Read ↗

Phosphate-binding loop and Rab GTPase function: mutations at Ser29 and Ala30 of Rab5 lead to loss-of-function as well as gain-of-function phenotype.Semantic proximity Read ↗

Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases.Semantic proximity Read ↗

Splice variants of SmgGDS control small GTPase prenylation and membrane localization.Semantic proximity Read ↗

Structure-function relationship of the small GTPase rab5.Semantic proximity Read ↗

[Structure and properties of Rab proteins].Semantic proximity Read ↗

Farnesol modification of Kirsten-ras exon 4B protein is essential for transformation.Semantic proximity Read ↗

Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate.Semantic proximity Read ↗

Evidence for a symmetrical requirement for Rab5-GTP in in vitro endosome-endosome fusion.Semantic proximity Read ↗

Dimerization of small GTPase Rab5.Semantic proximity Read ↗

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