The intracellular redox protein MICAL-1 regulates the development of hippocampal mossy fibre connections

Battum, Eljo Y. van; Gunput, Rou-Afza F.; Lemstra, Suzanne; Groen, Ewout J N; Yu, Ka Lou; Adolfs, Youri; Zhou, Yun; Hoogenraad, Casper C.; Yoshida, Yukata; Schachner, Melitta; Akhmanova, Anna; Pasterkamp, R. Jeroen

doi:10.1038/ncomms5317

Cited by 60 publications

(89 citation statements)

References 70 publications

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“…For example, Drosophila MICAL is identified as an essential for neuronal growth by interactions with the cytoplasmic region of plexin and activating plexin‐ and semaphorin‐mediated axonal signalling 20. Recent studies also reported that MICAL1 promoted the development of hippocampal mossy fibre connections through its ability to control actin cytoskeleton rearrangement 21. The notion that cell cytoskeleton rearrangement contributes to cell proliferation has been confirmed by many research groups15; however, up to now, no study yet addressed the function of MICAL1 in the human cancer cell proliferation process.…”

Section: Discussionmentioning

confidence: 99%

MICAL1 facilitates breast cancer cell proliferation via ROS‐sensitive ERK/cyclin D pathway

Deng

Wang

Zhao

et al. 2018

J Cellular Molecular Medi

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Molecule interacting with CasL 1 (MICAL1) is a multidomain flavoprotein mono‐oxygenase that strongly involves in cytoskeleton dynamics and cell oxidoreduction metabolism. Recently, results from our laboratory have shown that MICAL1 modulates reactive oxygen species (ROS) production, and the latter then activates phosphatidyl inositol 3‐kinase (PI3K)/protein kinase B (Akt) signalling pathway which regulates breast cancer cell invasion. Herein, we performed this study to assess the involvement of MICAL1 in breast cancer cell proliferation and to explore the potential molecular mechanism. We noticed that depletion of MICAL1 markedly reduced cell proliferation in breast cancer cell line MCF‐7 and T47D. This effect of MICAL1 on proliferation was independent of wnt/β‐catenin and NF‐κB pathways. Interestingly, depletion of MICAL1 significantly inhibited ROS production, decreased p‐ERK expression and unfavourable for proliferative phenotype of breast cancer cells. Likewise, MICAL1 overexpression increased p‐ERK level as well as p‐ERK nucleus translocation. Moreover, we investigated the effect of MICAL1 on cell cycle‐related proteins. MICAL1 positively regulated CDK4 and cyclin D expression, but not CDK2, CDK6, cyclin A and cyclin E. In addition, more expression of CDK4 and cyclin D by MICAL1 overexpression was blocked by PI3K/Akt inhibitor LY294002. LY294002 treatment also attenuated the increase in the p‐ERK level in MICAL1‐overexpressed breast cancer cells. Together, our results suggest that MICAL1 exhibits its effect on proliferation via maintaining cyclin D expression through ROS‐sensitive PI3K/Akt/ERK signalling in breast cancer cells.

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Section: Discussionmentioning

confidence: 99%

MICAL1 facilitates breast cancer cell proliferation via ROS‐sensitive ERK/cyclin D pathway

Deng

Wang

Zhao

et al. 2018

J Cellular Molecular Medi

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“…It appears that Mical1 is a negative regulator of apoptosis, wherein inhibition of Mical1 induced rapid NDR-dependent (nuclear Dbf2-related kinase) apoptosis in melanoma cells (39). Another report demonstrated that Mical1, through redox regulation of actin cytoskeleton, controls the intracellular distribution of secretory vesicles that, in turn, regulates growth cone membrane targeting of the cell adhesion molecule (IgCAMs) in neurons (67). Therefore, it appears that Mical1 controls the development of lamina-restricted hippocampal moss fiber connection.…”

Section: Stereospecific Regulation Of Meto By Selenoprotein Msrb1mentioning

confidence: 99%

Regulation of Protein Function by Reversible Methionine Oxidation and the Role of Selenoprotein MsrB1

Kaya

Lee

Gladyshev

2015

Antioxidants & Redox Signaling

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Significance: Protein structure and function can be regulated via post-translational modifications by numerous enzymatic and nonenzymatic mechanisms. Regulation involving oxidation of sulfur-containing residues emerged as a key mechanism of redox control. Unraveling the participants and principles of such regulation is necessary for understanding the biological significance of redox control of cellular processes. Recent Advances: Reversible oxidation of methionine residues by monooxygenases of the Mical family and subsequent reduction of methionine sulfoxides by a selenocysteine-containing methionine sulfoxide reductase B1 (MsrB1) was found to control the assembly and disassembly of actin in mammals, and the Mical/MsrB pair similarly regulates actin in fruit flies. This finding has opened up new avenues for understanding the use of stereospecific methionine oxidation in regulating cellular processes and the roles of MsrB1 and Micals in regulation of actin dynamics. Critical Issues: So far, Micals have been the only known partners of MsrB1, and actin is the only target. It is important to identify additional substrates of Micals and characterize other Mical-like enzymes. Future Directions: Oxidation of methionine, reviewed here, is an emerging but not well-established mechanism. Studies suggest that methionine oxidation is a form of oxidative damage of proteins, a modification that alters protein structure or function, a tool in redox signaling, and a mechanism that controls protein function. Understanding the functional impact of reversible oxidation of methionine will require identification of targets, substrates, and regulators of Micals and Msrs. Linking the biological processes, in which these proteins participate, might also lead to insights into disease conditions, which involve regulation of actin by Micals and Msrs. Antioxid. Redox Signal. 23,[814][815][816][817][818][819][820][821][822]

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“…Numerous mossy fiber terminals were seen scattered within the pyramidal cell layer in Chl1 ¡/¡ mice, suggesting that the terminals were formed not only on proximal dendrites of the pyramidal cells, but also on the cell bodies. 26,27,36 Interestingly, NCAM-deficient animals also have demonstrated similar abnormal projections of mossy fibers in the hippocampus. 25 However, we did not observe an increased mossy fiber invasion into the SP of Cntn6 ¡/¡ mice, but rather an increase in length and size of mossy fiber projections in the SPB.…”

Section: Discussionmentioning

confidence: 99%

“…The fasciculation of efferents of this system is sensitive to alterations in axon guidance molecules and CAMs. 26,27,[34][35][36] In the hippocampus of P14 and adult mice, there was low Cntn6 mRNA expression in the pyramidal neurons of CA1 and CA3, in the granular neurons of the DG and in the dispersed cell bodies inside the hilus of the DG (Fig. 1C).…”

Section: Differential Spatiotemporal Expression Of Cntn6 In the Brainmentioning

confidence: 99%

Developmental role of the cell adhesion molecule Contactin-6 in the cerebral cortex and hippocampus

Zuko

Oguro-Ando

et al. 2016

Cell Adhesion & Migration

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The gene encoding the neural cell adhesion molecule Contactin-6 (Cntn6 a.k.a. NB-3) has been implicated as an autism risk gene, suggesting that its mutation is deleterious to brain development. Due to its GPI-anchor at Cntn6 may exert cell adhesion/receptor functions in complex with other membrane proteins, or serve as a ligand. We aimed to uncover novel phenotypes related to Cntn6 functions during development in the cerebral cortex of adult Cntn6 ¡/¡ mice. We first determined Cntn6 protein and mRNA expression in the cortex, thalamic nuclei and the hippocampus at P14, which decreased specifically in the cortex at adult stages. Neuroanatomical analysis demonstrated a significant decrease of Cux1C projection neurons in layers II-IV and an increase of FoxP2C projection neurons in layer VI in the visual cortex of adult Cntn6 ¡/¡ mice compared to wild-type controls. Furthermore, the number of parvalbuminC (PV) interneurons was decreased in Cntn6 ¡/¡ mice, while the amount of NPYC interneurons remained unchanged. In the hippocampus the delineation and outgrowth of mossy fibers remained largely unchanged, except for the observation of a larger suprapyramidal bundle. The observed abnormalities in the cerebral cortex and hippocampus of Cntn6 ¡/¡ mice suggests that Cntn6 serves developmental functions involving cell survival, migration and fasciculation. Furthermore, these data suggest that Cntn6 engages in both trans-and cis-interactions and may be involved in larger protein interaction networks.

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The intracellular redox protein MICAL-1 regulates the development of hippocampal mossy fibre connections

Cited by 60 publications

References 70 publications

MICAL1 facilitates breast cancer cell proliferation via ROS‐sensitive ERK/cyclin D pathway

MICAL1 facilitates breast cancer cell proliferation via ROS‐sensitive ERK/cyclin D pathway

Regulation of Protein Function by Reversible Methionine Oxidation and the Role of Selenoprotein MsrB1

Developmental role of the cell adhesion molecule Contactin-6 in the cerebral cortex and hippocampus

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