ArticleThe Journal of biological chemistry2009
The phox domain of sorting nexin 5 lacks phosphatidylinositol 3-phosphate (PtdIns(3)P) specificity and preferentially binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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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.
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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- Structural determinants specific for retromer protein sorting nexin 5 in regulating subcellular retrograde membrane trafficking.Journal of biomedical research · 2023Article
- Out of the ESCPE room: Emerging roles of endosomal SNX-BARs in receptor transport and host-pathogen interaction.Traffic (Copenhagen, Denmark) · 2023Review
- The association of lipid transfer protein VPS13A with endosomes is mediated by sorting nexin SNX5.Life science alliance · 2023Article
- Lysine acetylation regulates the interaction between proteins and membranes.Nature communications · 2021Article
- Sorting Out Sorting Nexins Functions in the Nervous System in Health and Disease.Molecular neurobiology · 2021Review
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- Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment.Frontiers in cell and developmental biology · 2021Article
- Mechanism of cargo recognition by retromer-linked SNX-BAR proteins.PLoS biology · 2020Article
- Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities.Nature communications · 2019Article
- Comparative Characterization of the Sindbis Virus Proteome from Mammalian and Invertebrate Hosts Identifies nsP2 as a Component of the Virion and Sorting Nexin 5 as a Significant Host Factor for Alphavirus Replication.Journal of virology · 2018Article
- Article
- Phosphorylation of conserved phosphoinositide binding pocket regulates sorting nexin membrane targeting.Nature communications · 2018Article
- Phosphoinositides, Major Actors in Membrane Trafficking and Lipid Signaling Pathways.International journal of molecular sciences · 2017Review
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- Article
- Emerging roles of PtdIns(4,5)P2--beyond the plasma membrane.Journal of cell science · 2015Review
- Global Mapping of the Inc-Human Interactome Reveals that Retromer Restricts Chlamydia Infection.Cell host & microbe · 2015Article
- PIP kinases define PI4,5P₂signaling specificity by association with effectors.Biochimica et biophysica acta · 2015Review
- Asymmetric binding to NS5A by daclatasvir (BMS-790052) and analogs suggests two novel modes of HCV inhibition.Journal of medicinal chemistry · 2014Article
- Structural basis for different phosphoinositide specificities of the PX domains of sorting nexins regulating G-protein signaling.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
Subcellular retrograde transport of cargo receptors from endosomes to the trans-Golgi network is critically involved in a broad range of physiological and pathological processes and highly regulated by a genetically conserved heteropentameric complex, termed retromer. Among the retromer components identified in mammals, sorting nexin 5 and 1 (SNX5; SNX1) have recently been found to interact, possibly controlling the membrane binding specificity of the complex. To elucidate how the unique sequence features of the SNX5 phox domain (SNX5-PX) influence retrograde transport, we have determined the SNX5-PX structure by NMR and x-ray crystallography at 1.5 A resolution. Although the core fold of SNX5-PX resembles that of other known PX domains, we found novel structural features exclusive to SNX5-PX. It is most noteworthy that in SNX5-PX, a long helical hairpin is added to the core formed by a new alpha2'-helix and a much longer alpha3-helix. This results in a significantly altered overall shape of the protein. In addition, the unique double PXXP motif is tightly packed against the rest of the protein, rendering this part of the structure compact, occluding parts of the putative phosphatidylinositol (PtdIns) binding pocket. The PtdIns binding and specificity of SNX5-PX was evaluated by NMR titrations with eight different PtdIns and revealed that SNX5-PX preferentially and specifically binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)). The distinct structural and PtdIns binding characteristics of SNX5-PX impart specific properties on SNX5, influencing retromer-mediated regulation of retrograde trafficking of transmembrane cargo receptors.
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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.