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

Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells.

Journal of cell science - 1 Dec 2004

Malinska Katerina, Malinsky Jan, Opekarova Miroslava, Tanner Widmar

Abstract excerpt

Recently, lipid-raft-based subdomains within the plasma membrane of living Saccharomyces cerevisiae cells were visualized using green fluorescent protein fusions, and non-overlapping subdomains containing either Pma1p or Can1p were distinguished. In this study, the long-term stability of the subdomains was investigated. Experiments with latrunculin A and nocodazole ruled out the involvement of cytoskeletal...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Transport Systems
Share to Amino Acid Transport Systems, Basic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Detergents

Share to Marine Toxins

Share to Membrane Microdomains

Share to Nocodazole

Share to Octoxynol

Share to Thiazolidines

Source

Identifiers

PMID: 15536122
DOI: 10.1242/jcs.01493

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells.PMID 15536122Read ↗

Sphingolipid levels crucially modulate lateral microdomain organization of plasma membrane in living yeast.Semantic proximity Read ↗

Very long-chain fatty acid-containing lipids rather than sphingolipids per se are required for raft association and stable surface transport of newly synthesized plasma membrane ATPase in yeast.Semantic proximity Read ↗

Plasma membrane microdomains regulate turnover of transport proteins in yeast.Semantic proximity Read ↗

Furrow-like invaginations of the yeast plasma membrane correspond to membrane compartment of Can1.Semantic proximity Read ↗

Rapid multiplex analysis of lipid raft components with single-cell resolution.Semantic proximity Read ↗

Raft partitioning of the yeast uracil permease during trafficking along the endocytic pathway.Semantic proximity Read ↗

Lipid-dependent surface transport of the proton pumping ATPase: a model to study plasma membrane biogenesis in yeast.Semantic proximity Read ↗

The uracil transporter Fur4p associates with lipid rafts.Semantic proximity Read ↗

Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae.Semantic proximity Read ↗

The fidgety yeast: focus on high-resolution live yeast cell microscopy.Semantic proximity Read ↗

HAP1 and intracellular traffickingSemantic proximity Read ↗

Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis.Semantic proximity Read ↗

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