ArticleThe Journal of biological chemistry2012
Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 14 papers.
What it found
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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.
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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
14 citing papers in PubMed, 34 citations in OpenAlex.
- Histone phosphorylation analysis of two main TCM syndromes of chronic fatigue syndrome.Journal of translational medicine · 2025Article
- A High-Resolution Map of SBP1 Interactomes in Plasmodium falciparum-infected Erythrocytes.iScience · 2019Article
- The membrane palmitoylated protein, MPP6, is involved in myelin formation in the mouse peripheral nervous system.Histochemistry and cell biology · 2019Article
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
- The mystery of membrane organization: composition, regulation and roles of lipid rafts.Nature reviews. Molecular cell biology · 2017Review
- Protein palmitoylation: Palmitoyltransferases and their specificity.Experimental biology and medicine (Maywood, N.J.) · 2017Article
- Protein Palmitoylation and Its Role in Bacterial and Viral Infections.Frontiers in immunology · 2017Review
- The Schistosome Esophagus Is a 'Hotspot' for Microexon and Lysosomal Hydrolase Gene Expression: Implications for Blood Processing.PLoS neglected tropical diseases · 2015Article
- MPP1 as a Factor Regulating Phase Separation in Giant Plasma Membrane-Derived Vesicles.Biophysical journal · 2015Article
- Co-operation of TLR4 and raft proteins in LPS-induced pro-inflammatory signaling.Cellular and molecular life sciences : CMLS · 2015Review
- Acanthocytosis and the c.680 A>G Mutation in the PANK2 Gene: A Study Enrolling a Cohort of PKAN Patients from the Dominican Republic.PloS one · 2015Article
- Common and distinctive localization patterns of Crumbs polarity complex proteins in the mammalian eye.Gene expression patterns : GEP · 2015Article
- Cholesterol Interaction with the MAGUK Protein Family Member, MPP1, via CRAC and CRAC-Like Motifs: An In Silico Docking Analysis.PloS one · 2015Article
- Hematopoietic protein-1 regulates the actin membrane skeleton and membrane stability in murine erythrocytes.PloS one · 2013Article
Corrections and comments
- Retraction · 2018-02-23Concerns/Issues about Data · Concerns/Issues about Image ·
- Retracted
Authors and funding
15 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
S-Acylation of proteins is a ubiquitous post-translational modification and a common signal for membrane association. The major palmitoylated protein in erythrocytes is MPP1, a member of the MAGUK family and an important component of the ternary complex that attaches the spectrin-based skeleton to the plasma membrane. Here we show that DHHC17 is the only acyltransferase present in red blood cells (RBC). Moreover, we give evidence that protein palmitoylation is essential for membrane organization and is crucial for proper RBC morphology, and that the effect is specific for MPP1. Our observations are based on the clinical cases of two related patients whose RBC had no palmitoylation activity, caused by a lack of DHHC17 in the membrane, which resulted in a strong decrease of the amount of detergent-resistant membrane (DRM) material. We confirmed that this loss of detergent-resistant membrane was due to the lack of palmitoylation by treatment of healthy RBC with 2-bromopalmitic acid (2-BrP, common palmitoylation inhibitor). Concomitantly, fluorescence lifetime imaging microscopy (FLIM) analyses of an order-sensing dye revealed a reduction of membrane order after chemical inhibition of palmitoylation in erythrocytes. These data point to a pathophysiological relationship between the loss of MPP1-directed palmitoylation activity and perturbed lateral membrane organization.
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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.