ArticleThe Journal of biological chemistry2014
Structural basis for different phosphoinositide specificities of the PX domains of sorting nexins regulating G-protein signaling.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 48 citations in OpenAlex.
- SNX11 Deletion Inhibits Dabie bandavirus Infection by Interfering with the Assembly of V-ATPase.Pathogens (Basel, Switzerland) · 2025Article
- SNX19 Interacts with Caveolin-1 and Flotillin-1 to Regulate DBiomedicines · 2025Article
- Assembly and fission of tubular carriers mediating protein sorting in endosomes.Nature reviews. Molecular cell biology · 2024Review
- Transmembrane Membrane Readers form a Novel Class of Proteins That Include Peripheral Phosphoinositide Recognition Domains and Viral Spikes.Membranes · 2022Review
- Lipid Dyshomeostasis and Inherited Cerebellar Ataxia.Molecular neurobiology · 2022Review
- Structural Predictions of the SNX-RGS Proteins Suggest They Belong to a New Class of Lipid Transfer Proteins.Frontiers in cell and developmental biology · 2022Article
- 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
- SNX19 restricts endolysosome motility through contacts with the endoplasmic reticulum.Nature communications · 2021Article
- Towards a better understanding of the neuro-developmental role of autophagy in sickness and in health.Cell stress · 2021Review
- Article
- Attracted to membranes: lipid-binding domains in plants.Plant physiology · 2021Article
- SNX-PXA-RGS-PXC Subfamily of SNXs in the Regulation of Receptor-Mediated Signaling and Membrane Trafficking.International journal of molecular sciences · 2021Review
- A Unique Junctional Interface at Contact Sites Between the Endoplasmic Reticulum and Lipid Droplets.Frontiers in cell and developmental biology · 2021Review
- Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment.Frontiers in cell and developmental biology · 2021Article
- Lipid rafts are required for effective renal DFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Schizophrenia risk variants influence multiple classes of transcripts of sorting nexin 19 (SNX19).Molecular psychiatry · 2020Article
- Emerging Role of the Autophagy/Lysosomal Degradative Pathway in Neurodevelopmental Disorders With Epilepsy.Frontiers in cellular neuroscience · 2020Article
- Drosophila Snazarus Regulates a Lipid Droplet Population at Plasma Membrane-Droplet Contacts in Adipocytes.Developmental cell · 2019Article
- Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities.Nature communications · 2019Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sorting nexins (SNXs) or phox homology (PX) domain containing proteins are central regulators of cell trafficking and signaling. A subfamily of PX domain proteins possesses two unique PX-associated domains, as well as a regulator of G protein-coupled receptor signaling (RGS) domain that attenuates Gαs-coupled G protein-coupled receptor signaling. Here we delineate the structural organization of these RGS-PX proteins, revealing a protein family with a modular architecture that is conserved in all eukaryotes. The one exception to this is mammalian SNX19, which lacks the typical RGS structure but preserves all other domains. The PX domain is a sensor of membrane phosphoinositide lipids and we find that specific sequence alterations in the PX domains of the mammalian RGS-PX proteins, SNX13, SNX14, SNX19, and SNX25, confer differential phosphoinositide binding preferences. Although SNX13 and SNX19 PX domains bind the early endosomal lipid phosphatidylinositol 3-phosphate, SNX14 shows no membrane binding at all. Crystal structures of the SNX19 and SNX14 PX domains reveal key differences, with alterations in SNX14 leading to closure of the binding pocket to prevent phosphoinositide association. Our findings suggest a role for alternative membrane interactions in spatial control of RGS-PX proteins in cell signaling and trafficking.
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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.