ArticleThe EMBO journal2007
Structure of Sla1p homology domain 1 and interaction with the NPFxD endocytic internalization motif.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- The non-catalytic DNA polymerase ε subunit is an NPF motif recognition protein.Nature communications · 2025Article
- Competitive binding of actin and SH3 domains at proline-rich regions of Las17/WASP regulates actin polymerisation.Communications biology · 2025Article
- Essential role of the endocytic site-associated protein Ecm25 in stress-induced cell elongation.Cell reports · 2021Article
- Cargo-mediated recruitment of the endocytic adaptor protein Sla1 inJournal of cell science · 2020Article
- GPCR receptor phosphorylation and endocytosis are not necessary to switch polarized growth between internal cues during pheromone response inCommunicative & integrative biology · 2020Article
- The Sla1 adaptor-clathrin interaction regulates coat formation and progression of endocytosis.Traffic (Copenhagen, Denmark) · 2018Article
- Article
- A second Las17 monomeric actin-binding motif functions in Arp2/3-dependent actin polymerization during endocytosis.Traffic (Copenhagen, Denmark) · 2015Article
- Calcineurin regulates the yeast synaptojanin Inp53/Sjl3 during membrane stress.Molecular biology of the cell · 2015Article
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- Specific α-arrestins negatively regulate Saccharomyces cerevisiae pheromone response by down-modulating the G-protein-coupled receptor Ste2.Molecular and cellular biology · 2014Article
- SLAC, a complex between Sla1 and Las17, regulates actin polymerization during clathrin-mediated endocytosis.Molecular biology of the cell · 2012Article
- Role of Scd5, a protein phosphatase-1 targeting protein, in phosphoregulation of Sla1 during endocytosis.Journal of cell science · 2012Article
- In vivo andin vitro studies of adaptor-clathrin interaction.Journal of visualized experiments : JoVE · 2011Article
- Regulation of clathrin adaptor function in endocytosis: novel role for the SAM domain.The EMBO journal · 2010Article
- Structural basis for ubiquitin recognition by SH3 domains.Journal of molecular biology · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Adaptor proteins play important endocytic roles including recognition of internalization signals in transmembrane cargo. Sla1p serves as the adaptor for uptake of transmembrane proteins containing the NPFxD internalization signal, and is essential for normal functioning of the actin cytoskeleton during endocytosis. The Sla1p homology domain 1 (SHD1) within Sla1p is responsible for recognition of the NPFxD signal. This study presents the NMR structure of the NPFxD-bound state of SHD1 and a model for the protein-ligand complex. The alpha+beta structure of the protein reveals an SH3-like topology with a solvent-exposed hydrophobic ligand binding site. NMR chemical shift perturbations and effects of structure-based mutations on ligand binding in vitro define residues that are key for NPFxD binding. Mutations that abolish ligand recognition in vitro also abolish NPFxD-mediated receptor internalization in vivo. Thus, SHD1 is a novel functional domain based on SH3-like topology, which employs a unique binding site to recognize the NPFxD endocytic internalization signal. Its distant relationship with the SH3 fold endows this superfamily with a new role in endocytosis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.