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

An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast.

Journal of cell science - 15 Jun 2003

Gourlay Campbell W, Dewar Hilary, Warren Derek T, Costa Rosaria, Satish Nilima, Ayscough Kathryn R

Abstract excerpt

The importance of a dynamic actin cytoskeleton for facilitating endocytosis has been recognised for many years in budding yeast and is increasingly recognised in mammalian cells. However, the mechanism for actin recruitment and the role it plays in endocytosis is unclear. Here we show the importance of two yeast proteins in this process. We demonstrate that Sla1p and Sla2p interact in vitro and in vivo and that...

Read the complete abstract on PubMed

Topics

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

Share to Actin Cytoskeleton
Share to Bridged Bicyclo Compounds, Heterocyclic

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

Share to Macromolecular Substances

Share to Thiazoles

Share to Thiazolidines

Share to Transport Vesicles

Share to Vacuoles

Share to Wiskott-Aldrich Syndrome Protein

Source

Identifiers

PMID: 12734398
DOI: 10.1242/jcs.00454

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

An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast.PMID 12734398Read ↗

Interaction of Sla2p's ANTH domain with PtdIns(4,5)P2 is important for actin-dependent endocytic internalization.Semantic proximity Read ↗

Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology.Semantic proximity Read ↗

Novel proteins linking the actin cytoskeleton to the endocytic machinery in Saccharomyces cerevisiae.Semantic proximity Read ↗

An Abp1-dependent route of endocytosis functions when the classical endocytic pathway in yeast is inhibited.Semantic proximity Read ↗

Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals.Semantic proximity Read ↗

Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of sla2p in yeast.Semantic proximity Read ↗

Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae.Semantic proximity Read ↗

Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions.Semantic proximity Read ↗

Role of Scd5, a protein phosphatase-1 targeting protein, in phosphoregulation of Sla1 during endocytosis.Semantic proximity Read ↗

The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae.Semantic proximity Read ↗

Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis.Semantic proximity Read ↗

Molecular basis for coupling the plasma membrane to the actin cytoskeleton during clathrin-mediated endocytosis.Semantic proximity Read ↗

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