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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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EFA6 proteins regulate lumen formation through α-actinin 1.

Julie Milanini1, Racha Fayad1, Mariagrazia Partisani1

  • 1Université Côte d'Azur, CNRS, Institut de Pharmacologie Moléculaire et Cellulaire (IPMC), Valbonne, F-06560, France.

Journal of Cell Science
|December 17, 2017
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Summary

Epithelial lumen formation relies on EFA6A and alpha-actinin 1 (ACTN1) proteins. These proteins regulate cell contractility, essential for lumen growth and maturation in epithelial morphogenesis.

Keywords:
ACTN1ContractilityEFA6EpitheliumLumen

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Area of Science:

  • Cell Biology
  • Developmental Biology
  • Epithelial Biology

Background:

  • Epithelial morphogenesis involves lumen formation, a critical process for organ development.
  • Luminogenesis, or lumen creation, occurs through vesicle fusion and lumen expansion.

Purpose of the Study:

  • To investigate the role of EFA6A and its interacting partners in epithelial luminogenesis.
  • To identify novel regulators involved in the maturation of newly formed lumens.

Main Methods:

  • Utilized Madin-Darby canine kidney (MDCK) cells in 3D culture to model luminogenesis.
  • Employed co-immunoprecipitation to identify protein interactions.
  • Investigated protein function through manipulation in cell culture models.

Main Results:

  • Discovered that EFA6A recruits alpha-actinin 1 (ACTN1) and is crucial for luminogenesis.
  • Demonstrated that ACTN1, enriched at tight junctions, is a key effector of EFA6A in lumen extension and enlargement.
  • Showed that EFA6A and ACTN1 regulate cortical acto-myosin contractility.
  • Identified EFA6B as an effector of ACTN1 in restoring glandular morphology in MCF7 cells.

Conclusions:

  • EFA6A and ACTN1 are essential regulators of epithelial lumen formation and maturation.
  • These proteins mediate their function by controlling acto-myosin contractility at the cell cortex.
  • The findings reveal new molecular players in epithelial morphogenesis and potential therapeutic targets.