PLSCR4

Last update 08 May 2025

Basic Info

Synonyms

Ca(2+)-dependent phospholipid scramblase 4, Cell growth-inhibiting gene 43 protein, phospholipid scramblase 4

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Introduction

Catalyzes metal ion-induced ATP-independent rapid bidirectional and non-specific movement of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane and participates in the redistribution of phospholipids between membrane leaflets (PubMed:23089641). Metal ions bind to the calcium-binding site and induce conformation change in the protein (PubMed:23089641). Has a greater affi nity for Ca(2+) than Mg(2+) and Zn(2+) (PubMed:23089641).

100 Clinical Results associated with PLSCR4

100 Translational Medicine associated with PLSCR4

0 Patents (Medical) associated with PLSCR4

Literatures (Medical) associated with PLSCR4

01 Feb 2025·Cancer Biomarkers

Biomarkers and potential function analysis of triple-negative breast cancer screening based on bioinformatics

Article

Author: Li, Dan ; Yang, Yang ; Wang, Xiaoli ; Guo, Wenjia ; Chen, Lin ; Zhou, Duanfang ; Tan, Xiaodan ; Chen, Xing ; Peng, Zhe

This study aims to identify and validate potential endogenous biomarkers for triple-negative breast cancer (TNBC). TNBC microarray data (GSE38959, GSE53752) were retrieved from the Gene Expression Omnibus (GEO) database, and principal component analysis (PCA) was performed to evaluate the reliability of the data. The microarray datasets were merged, and differentially expressed genes (DEGs) were identified using R software. Functional enrichment analysis of the DEGs was conducted using Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways. The most disease-relevant module was identified through Weighted Gene Co-expression Network Analysis (WGCNA), and genes within this module were intersected with the DEGs. The intersecting genes underwent Least Absolute Shrinkage and Selection Operator (LASSO) regression analysis to minimize errors and identify TNBC-specific genes. Sensitivity and survival analyses were performed on the identified specific genes. There were 10 TNBC-specific genes identified: RRM2, DEPDC1, FIGF, TACC3, E2F1, CDO1, DST, MCM4, CHEK1, and PLSCR4. RT-qPCR analysis showed significant upregulation of CDO1, MCM4, DEPDC1, RRM2, and E2F1 in MDA-MB-231, CAL-148, and MFM-223 compared to MCF-10A. Our findings provide new insights into TNBC pathogenesis and potential therapeutic strategies, with important clinical implications for further understanding TNBC mechanisms and developing innovative treatments.

12 Jun 2024·Biological and Pharmaceutical Bulletin

Phospholipid Scramblase 1 Localizes Proximal to Sphingomyelin Synthase Isoforms but Is Not Involved in Sphingomyelin Synthesis

Article

Author: Horioka, Naoto ; Suzuki, Takehiro ; Dohmae, Naoshi ; Hayashi, Yasuhiro ; Tanikawa, Takashi

Ceramide (Cer) is synthesized de novo in the bilayer of the endoplasmic reticulum and transported to the cytosolic leaflet of the trans-Golgi apparatus for sphingomyelin (SM) synthesis. As the active site of SM synthase (SMS) is located on the luminal side of the Golgi membrane, Cer translocates to the lumen via transbilayer movement for SM synthesis. However, the mechanism of transbilayer movement is not fully understood. As the Cer-related translocases seem to localize near the SMS, the protein was identified using proximity-dependent biotin identification proteomics. Phospholipid scramblase 1 (PLSCR1), which is thought to act as a scramblase for phosphatidylserine and phosphatidylethanolamine, was identified as a protein proximal to the SMS isoforms SMS1 and SMS2. Although five isoforms of PLSCR have been reported in humans, only PLSCR1, PLSCR3, and PLSCR4 are expressed in HEK293T cells. Confocal microscopic analysis showed that PLSCR1 and PLSCR4 partially co-localized with p230, a trans-Golgi network marker, where SMS isoforms are localized. We established CRISPR/Cas9-mediated PLSCR1, PLSCR3, and PLSCR4 single-knockout cells and PLSCR1, 3, 4 triple knockout HEK293T cells. Liquid chromatography-tandem mass spectrometry revealed that the levels of species with distinct acyl chains in Cer and SM were not significantly different in single knockout cells or in the triple knockout cells compared to the wild-type cells. Our findings suggest that PLSCR1 is localized in the vicinity of SMS isoforms, however is not involved in the transbilayer movement of Cer for SM synthesis.

01 May 2024·International Journal of Biological Macromolecules

MiR-103-5p deficiency suppresses lipid accumulation via upregulating PLSCR4 and its host gene PANK3 in goat mammary epithelial cells

Article

Author: Luo, Jun ; Lu, Xuefeng ; Gong, Ping ; Gao, Wenchang ; Zhu, Lu ; Zhang, Fuhong ; Zhao, Jianqing ; Liu, Baolong ; Jiao, Hongyun ; Shi, Chenbo

Lipids are intimately related to the unique flavor and nutritional values of goat milk. MicroRNAs (miRNA) participate in the regulation of various biological functions, including the synthesis and degradation of lipids. Several studies have shown that miR-103 is involved in the regulation of lipid metabolism, however, the molecular mechanism by which miR-103 regulates lipid metabolism in goat mammary gland is poorly understood. In this study, miR-103 was knocked out in goat mammary epithelial cells (GMECs) by CRISPR/Cas9, and the accumulation of lipid droplets, triglycerides, and cholesterol in the cells was suppressed subsequently. Overexpression or knockdown of miR-103-5p and miR-103-3p in GMECs revealed that it was miR-103-5p that promoted lipid accumulation but not miR-103-3p. In addition, Pantothenate Kinase 3 (PANK3), the host gene of miR-103, and Phospholipid Scramblase 4 (PLSCR4) were identified as the target genes of miR-103-5p by dual fluorescein and miRNA pulldown. Furthermore, we identified that cellular lipid levels were negatively regulated by PANK3 and PLSCR4. Lastly, in miR-103 knockout GMECs, the knockdown of PANK and PLSCR4 rescued the lipid accumulation. These findings suggest that miR-103-5p promotes lipid accumulation by targeting PLSCR4 and the host gene PANK3 in GMECs, providing new insights for the regulation of goat milk lipids via miRNAs.

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PLSCR4

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