bims-migras 2026-04-19 papers

Issue of 2026–04–19
two papers selected by
Cliff Dominy

J Cell Biol. 2026 Jun 01. pii: e202507023. [Epub ahead of print]225(6):

Palmitoylation of Tspan4 is essential for migrasome formation.

Shuonan Wang, Weisi Wang, Jiamei Qiao, Sadiq Ali, Zheng Jiang, Dong Jiang, Junjie Ma, Yuwei Huang.

Migrasomes are key organelles in cell-cell communication, playing a role in embryonic morphogenesis, angiogenesis, coagulation, and mitochondrial homeostasis. Migrasome formation involves the assembly of tetraspanin-enriched microdomains (TEMs) into larger macrodomains (TEMAs), but the underlying mechanisms are unclear. Here, we demonstrate that tetraspanin 4 (Tspan4) is highly palmitoylated at six juxtamembrane cysteines. DHHC6 and PPT1 are identified as the main enzymes regulating this modification. Palmitoylation of Tspan4 is critical for Tspan4 clustering and cholesterol recruitment, enabling the TEM to TEMA assembly required for migrasome formation and stabilization. Notably, the palmitoylation-deficient Tspan4 mutant acts in a dominant-negative manner, suppressing migrasome formation not only in cultured cells but also in zebrafish embryos, where it disrupts left-right asymmetry and organ morphogenesis. Collectively, our study establishes protein palmitoylation as a conserved and essential regulator of migrasome assembly, delineating a mechanism whereby Tspan4 palmitoylation drives cholesterol-dependent membrane macrodomain organization to enable migrasome formation and function.

DOI: https://doi.org/10.1083/jcb.202507023

J Extracell Vesicles. 2026 Apr;15(4): e70283

Magnetic-Assisted Aptamer Selection and Isolation of Migrasomes for Application in Lung Adenocarcinoma Proteomic Analysis.

Yixin Xu, Lin Jiao, Qiangying Yi, Yuzuo Chen, Bei Cai, Junlong Zhang, Zhuochun Huang, Yao Luo, Yanjun Si, Yao Wu, Binwu Ying, Jie Chen, Juan Zhou.

Migrasomes, newly discovered vesicular organelles, hold promise as diagnostic biomarkers and therapeutic targets in various diseases. However, the exploration of their clinical value remains hindered by the complexity of enriching and analyzing low concentrations of migrasomes in body fluids. To address this issue, a magnetic-assisted strategy was devised for screening aptamers specific to migrasomes, with the identified aptamer then being utilized for the specific isolation of migrasomes derived from clinical plasma. Initially, lipid-affinity magnetic nanoparticles were prepared and employed in a Magnetic-Systematic Evolution of Ligands by Exponential Enrichment (Mag-SELEX) process to identify aptamers that specifically target migrasomes. An optimal aptamer, Apt_B3, with a dissociation constant (Kd) of 251.9 nM, was successfully identified. This aptamer was subsequently utilized to construct the magnetic aptamer probe system, enabling the precise and rapid capture of migrasomes from plasma within 15 min. Our strategy exhibited exceptional separation efficiency, confirming its reliability and enhanced performance compared to traditional methods such as density gradient centrifugation. Clinical samples were then analyzed to validate the potential role of migrasome-derived tumor biomarkers in lung adenocarcinoma. These findings underscore the promising applicability of our strategy for studying migrasomes in clinical disease diagnosis.

Keywords: aptamer; lung adenocarcinoma; magnetic‐SELEX; migrasome; proteomic analysis

DOI: https://doi.org/10.1002/jev2.70283