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MICAL-L1 is required for cargo protein delivery to the cell surface

Abstract : Secreted proteins are transported along intracellular route from the endoplasmic reticulum through the Golgi before reaching the plasma membrane. Small GTPase Rab and their effectors play a key role in membrane trafficking. Using confocal microscopy, we showed that MICAL-L1 was associated with tubulo-vesicular structures and exhibited a significant colocalization with markers of the Golgi apparatus and recycling endosomes. Super resolution STORM microscopy suggested at the molecular level, a very close association of MICAL-L1 and microdomains in the Golgi cisternae. Using a synchronized secretion assay, we report that the shRNAmediated depletion of MICAL-L1 impaired the delivery of a subset of cargo proteins to the cell surface. The process of membrane tubulation was monitored in vitro, and we observe that recombinant MICAL-L1-RBD domain may contribute to promote PACSINsmediated membrane tubulation. Interestingly, two hydrophobic residues at the C-terminus of MICAL-L1 appeared to be important for phosphatidic acid binding, and for association with membrane tubules. Our results reveal a new role for MICAL-L1 in cargo delivery to the plasma membrane.
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Submitted on : Friday, June 11, 2021 - 3:25:48 PM
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Long-term archiving on: : Sunday, September 12, 2021 - 7:58:28 PM


Sikora et al. Biol Open 2021.p...
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R. Sikora, P. Bun, L. Danglot, M. Alqabandi, P. Bassereau, et al.. MICAL-L1 is required for cargo protein delivery to the cell surface. Biology Open, Royal Society, 2021, 10 (6), pp.bio058008. ⟨10.1242/bio.058008⟩. ⟨inserm-03258482⟩



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