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MIM triggers formin to Arp2/3-based actin assembly in membrane remodeling in Drosophila embryos

Debasmita Mitra1, Georgina K Goddard2, Sanjana S1

  • 1Indian Institute of Science Education and Research Pune , Pune, India.

The Journal of Cell Biology
|January 27, 2026
PubMed

Insights

Missing-in-metastasis (MIM) protein drives cell membrane remodeling by promoting actin networks and endocytosis during Drosophila embryo development. MIM is crucial for cell division and membrane shaping.

Area of Science:

  • Cell Biology
  • Developmental Biology
  • Biochemistry

Background:

  • BAR domain-containing proteins regulate endocytosis and actin.
  • The role of these proteins in morphogenesis is not well understood.

Purpose of the Study:

  • Investigate the function of the I-BAR domain protein missing-in-metastasis (MIM) in Drosophila morphogenesis.
  • Elucidate MIM's role in actin remodeling and membrane dynamics during syncytial divisions.

Main Methods:

  • Utilized Drosophila embryos for studying syncytial divisions.
  • Investigated the effects of MIM depletion on actin networks and membrane protrusions.
  • Analyzed the localization of key proteins involved in actin polymerization and endocytosis.

Main Results:

  • MIM promotes branched actin network formation and endocytosis for plasma membrane remodeling.
  • MIM depletion disrupts furrow extension and leads to altered apical protrusions.
  • MIM integrates branched and bundled actin networks, balancing their dynamics.
  • MIM recruitment to the cortex drives endocytic membrane remodeling via Rac, WAVE, and Arp2/3 complex.

Conclusions:

  • MIM is essential for rapid, cyclical membrane remodeling during Drosophila syncytial divisions.
  • MIM acts as an integrator of actin dynamics and endocytosis.
  • These findings reveal MIM's critical role in morphogenesis.

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