ArticleBioinformatics (Oxford, England)2009
Phospholipid scramblases and Tubby-like proteins belong to a new superfamily of membrane tethered transcription factors.
Article in Bioinformatics (Oxford, England), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 88 citations in OpenAlex.
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- 3-D substructure search by transitive closure in AlphaFold database.Protein science : a publication of the Protein Society · 2025Article
- Phospholipid scramblase 1: a frontline defense against viral infections.Frontiers in cellular and infection microbiology · 2025Review
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- Molecular responses of agroinfiltrated Nicotiana benthamiana leaves expressing suppressor of silencing P19 and influenza virus-like particles.Plant biotechnology journal · 2024Review
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- Genome-wide investigation and expression profiling ofFrontiers in plant science · 2023Article
- Biophysical characterization of the DNA binding motif of human phospholipid scramblase 1.European biophysics journal : EBJ · 2022Article
- Tubby-like proteins (TLPs) transcription factor in different regulatory mechanism in plants: a review.Plant molecular biology · 2022Review
- Genome-Wide Identification, Characterization, and Expression Analysis of Tubby-like Protein (TLP) Gene Family Members in Woodland Strawberry (International journal of molecular sciences · 2022Article
- Genome-Wide Identification and Characterization of SoybeanInternational journal of molecular sciences · 2021Article
- Pb(II) Induces Scramblase Activation and Ceramide-Domain Generation in Red Blood Cells.Scientific reports · 2018Article
- Using HHsearch to tackle proteins of unknown function: A pilot study with PH domains.Traffic (Copenhagen, Denmark) · 2016Article
- Multifaceted Roles of ALG-2 in Ca(2+)-Regulated Membrane Trafficking.International journal of molecular sciences · 2016Review
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
motivationPhospholipid scramblases (PLSCRs) constitute a family of cytoplasmic membrane-associated proteins that were identified based upon their capacity to mediate a Ca(2+)-dependent bidirectional movement of phospholipids across membrane bilayers, thereby collapsing the normally asymmetric distribution of such lipids in cell membranes. The exact function and mechanism(s) of these proteins nevertheless remains obscure: data from several laboratories now suggest that in addition to their putative role in mediating transbilayer flip/flop of membrane lipids, the PLSCRs may also function to regulate diverse processes including signaling, apoptosis, cell proliferation and transcription. A major impediment to deducing the molecular details underlying the seemingly disparate biology of these proteins is the current absence of any representative molecular structures to provide guidance to the experimental investigation of their function.
resultsHere, we show that the enigmatic PLSCR family of proteins is directly related to another family of cellular proteins with a known structure. The Arabidopsis protein At5g01750 from the DUF567 family was solved by X-ray crystallography and provides the first structural model for this family. This model identifies that the presumed C-terminal transmembrane helix is buried within the core of the PLSCR structure, suggesting that palmitoylation may represent the principal membrane anchorage for these proteins. The fold of the PLSCR family is also shared by Tubby-like proteins. A search of the PDB with the HHpred server suggests a common evolutionary ancestry. Common functional features also suggest that tubby and PLSCR share a functional origin as membrane tethered transcription factors with capacity to modulate phosphoinositide-based signaling.
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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.