In structural biology and membrane protein research, the extraction, purification, and concentration of membrane proteins often face multiple challenges—low expression levels, poor stability, and a tendency to aggregate—each of which directly impacts the success of subsequent structural determination.
On July 20, 2026, the research teams of Professor Long Tao and Professor Han Han from Taikang Medical College (School of Basic Medical Sciences) at Wuhan University published an important study in Nature Communications titled "Structural basis of PLPP3‑mediated lipid phosphate dephosphorylation and its role in melanoma." Using cryo‑electron microscopy (cryo‑EM), the study resolved the tetrameric structure of human phospholipid phosphatase 3 (PLPP3), elucidated the molecular mechanisms of substrate binding and zinc ion inhibition, and combined cancer somatic mutation analysis with functional experiments to reveal the tumor‑suppressive role of PLPP3 in melanoma.
This marks another major achievement by the team in the same journal, following their previous structural elucidation of the vitamin B₁₂ transporter ABCD4‑LMBD1 complex. In both studies, the team used Membrane Solutions ultrafiltration centrifugal tubes to concentrate the target proteins, providing high‑quality samples for high‑resolution structural analysis.
Journal: Nature Communications
DOI: 10.1038/s41467‑026‑75824‑w
Impact Factor: 18.1
New Scientific Discovery: Structure and Function of the Phospholipid Phosphatase PLPP3
PLPP3 belongs to the phospholipid phosphatase family and regulates diverse physiological processes—including cell proliferation, migration, angiogenesis, and inflammation—by catalyzing the dephosphorylation of lipid signaling molecules such as phosphatidic acid (PA) and lysophosphatidic acid (LPA). The protein is highly expressed in tissues such as the lung and skin, and its dysfunction is closely associated with vascular inflammation and various cancers. In this study, the high‑resolution structure of PLPP3 was determined by cryo‑EM, with the following key findings:
Tetrameric Assembly:
PLPP3 exists as a homotetramer, with each subunit containing six transmembrane helices. The tetramer is primarily stabilized by hydrophobic interactions between subunits, with phospholipid molecules at the interface also contributing to assembly stability.
Substrate Recognition Mechanism:
The transmembrane region of each subunit forms a hydrophobic cleft that accommodates the lipid tails, while the extracellular domain forms a positively charged pocket that recognizes the phosphate group. This architecture confers broad substrate specificity to PLPP3, enabling the hydrolysis of various lipid phosphates including PA, LPA, and S1P.
Zinc Ion Inhibition:
A zinc ion at the catalytic center is coordinated by two conserved histidine residues, stabilizing an inactive conformation and suppressing enzymatic activity. Upon zinc removal, the substrate phosphate group moves closer to the catalytic center, promoting the reaction.
Tumor Suppressor Function in Melanoma:
Melanoma‑associated somatic mutations (R155H, S194F, R245C, D255G) are all located in the catalytic center and impair phosphatase activity. Both in vitro and in vivo experiments confirmed that wild‑type PLPP3 significantly suppresses tumor growth, while the mutants lose their tumor‑suppressive function, establishing PLPP3 as a tumor suppressor in melanoma.
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Ultrafiltration Centrifugal Tube: A Key Tool for Membrane Protein Purification
Addressing the challenges of low expression levels, poor stability, and aggregation tendencies of membrane proteins, Membrane Solutions ultrafiltration centrifugal tubes have become a trusted choice for the research team due to the following features:
High Retention Accuracy, Low Protein Binding, Recovery >90%
Precise retention performance combined with low protein binding design minimizes target protein loss, making it especially suitable for low‑abundance samples.
Excellent Biocompatibility and Safety
Extremely low extractables, biocompatibility meeting USP <87> requirements, and no interference with sensitive samples.
Two‑sided Vertical Membrane Design
Prevents membrane clogging, ultra‑low hold‑up volume, significantly improves centrifugation efficiency, and shortens experiment time.
Anti‑dry Locking Design
Prevents sample damage due to over‑centrifugation, ensuring stable and reliable experimental results.
Membrane Solutions Ultrafiltration Product Series
Beyond the ultrafiltration centrifugal filters used in this study, Membrane Solutions offers a complete ultrafiltration product portfolio, including centrifugal tubes, ultrafiltration cups, and ultrafiltration cassettes, covering processing volumes from 0.1 mL to 3000 mL, fully supporting cutting‑edge research across multiple disciplines.
Membrane Solutions: Empowering Structural Biology Research with Reliable Quality
From the ABCD4‑LMBD1 vitamin B12 transporter complex to the structural elucidation of PLPP3, Membrane Solutions ultrafiltration centrifugal tubes have consistently supported the Wuhan University team in achieving multiple significant breakthroughs in structural biology. Whether for gentle concentration of membrane protein complexes or efficient recovery of low‑abundance samples, the same product has demonstrated stable and reliable performance across diverse applications.
We firmly believe that reliable laboratory consumables are the technical cornerstone of scientific discovery. Membrane Solutions will continue to focus on separation and filtration technologies, providing stable, efficient, and safe concentration and purification solutions for structural biology, cell biology, oncology, and other fields, working alongside researchers to explore the mysteries of life and advance science.