2. Academic Validation
  3. Localized, highly efficient secretion of signaling proteins by migrasomes

Localized, highly efficient secretion of signaling proteins by migrasomes

  • Cell Res. 2024 Jun 25. doi: 10.1038/s41422-024-00992-7.
Haifeng Jiao 1,  Xiaopeng Li 2,  Ying Li 2,  Yuting Guo 3,  Xiaoyu Hu 2,  Takami Sho 2,  Yiqun Luo 2,  Jinyu Wang 4,  Huizhen Cao 4,  Wanqing Du 2,  Dong Li 3,  Li Yu 5
Affiliations

Affiliations

  • 1 State Key Laboratory of Membrane Biology, Tsinghua University-Peking University Joint Centre for Life Sciences, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing, China. jiaohaifeng7@163.com.
  • 2 State Key Laboratory of Membrane Biology, Tsinghua University-Peking University Joint Centre for Life Sciences, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing, China.
  • 3 National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
  • 4 SLSTU-Nikon Biological Imaging Center, Center of Biomedical Analysis, Tsinghua University, Beijing, China.
  • 5 State Key Laboratory of Membrane Biology, Tsinghua University-Peking University Joint Centre for Life Sciences, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University, Beijing, China. liyulab@mail.tsinghua.edu.cn.
PMID: 38918584 DOI: 10.1038/s41422-024-00992-7
Abstract

Migrasomes, enriched with signaling molecules such as chemokines, cytokines and angiogenic factors, play a pivotal role in the spatially defined delivery of these molecules, influencing critical physiological processes including organ morphogenesis and angiogenesis. The mechanism governing the accumulation of signaling molecules in migrasomes has been elusive. In this study, we show that secretory proteins, including signaling proteins, are transported into migrasomes by secretory carriers via both the constitutive and regulated secretion pathways. During cell migration, a substantial portion of these carriers is redirected to the rear of the cell and actively transported into migrasomes, driven by the actin-dependent motor protein Myosin-5a. Once at the migrasomes, these carriers fuse with the migrasome membrane through SNARE-mediated mechanisms. Inhibiting migrasome formation significantly reduces secretion, suggesting migrasomes as a principal secretion route in migrating cells. Our findings reveal a specialized, highly localized secretion paradigm in migrating cells, conceptually paralleling the targeted neurotransmitter release observed in neuronal systems.

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