MICALs in control of the cytoskeleton, exocytosis, and cell death

Zhou, Yun; Gunput, Rou-Afza F.; Adolfs, Youri; Pasterkamp, R. Jeroen

doi:10.1007/s00018-011-0787-2

Cited by 47 publications

(54 citation statements)

References 92 publications

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“…Semaphorins are known to control neuronal differentiation through various signaling pathways (Pasterkamp, 2012) and, intriguingly, both Ndr1 and Ndr2 have been shown to interact with MICAL-1 (molecule interacting with CasL-1), an enzyme that links semaphorins to F-actin rearrangement during axonal and dendritic growth. MICAL-1 inhibits Ndr1/2 by competing with Mst kinases for binding at the hydrophobic motif and it has been suggested that semaphorins may disinhibit the kinase by sequestering MICAL (Hung et al, 2010;Zhou et al, 2011). Ndr kinases and semaphorins thus seem to interact in the intracellular signaling pathways that lead to ␤1-integrin activation in differentiating neuronal cells.…”

Section: Discussionmentioning

confidence: 99%

The Serine/Threonine Kinase Ndr2 Controls Integrin Trafficking and Integrin-Dependent Neurite Growth

Rehberg¹,

Kliche

Madencioglu³

et al. 2014

J. Neurosci.

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Integrins have been implicated in various processes of nervous system development, including proliferation, migration, and differentiation of neuronal cells. In this study, we show that the serine/threonine kinase Ndr2 controls integrin-dependent dendritic and axonal growth in mouse hippocampal neurons. We further demonstrate that Ndr2 is able to induce phosphorylation at the activity-and trafficking-relevant site Thr

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Section: Discussionmentioning

confidence: 99%

The Serine/Threonine Kinase Ndr2 Controls Integrin Trafficking and Integrin-Dependent Neurite Growth

Rehberg¹,

Kliche

Madencioglu³

et al. 2014

J. Neurosci.

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“…Mical2 was found to localize to the nucleus. In humans and mice, Mical1 and Mical3 are detected in tissues such as brain, lung, spleen, and kidney (41,71), but they appear to be expressed in other tissues as well. The presence of different Micals in different cell types and compartments further highlights the diverse in vivo functions of this family of enzymes.…”

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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“…Human MICAL proteins have four conserved domains: an N-terminal flavin adenine dinucleotide (FAD) binding domain, a calponin homology (CH) domain, a Lin11, Isl-1 and Mec-3 (LIM) domain and a C-terminal coiled-coil (CC) domain (Fig. 1A) (reviewed by Hung and Terman, 2011;Zhou et al, 2011a). MICAL1 has the most closely related domain architecture to Drosophila MICAL, whereas MICAL3 displays the least homology (Fig.…”

Section: Introductionmentioning

confidence: 99%

Differential regulation of actin microfilaments by human MICAL proteins

Giridharan

Rohn

Naslavsky

et al. 2012

Journal of Cell Science

124

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SummaryThe Drosophila melanogaster MICAL protein is essential for the neuronal growth cone machinery that functions through plexin-and semaphorin-mediated axonal signaling. Drosophila MICAL is also involved in regulating myofilament organization and synaptic structures, and serves as an actin disassembly factor downstream of plexin-mediated axonal repulsion. In mammalian cells there are three known isoforms, MICAL1, MICAL2 and MICAL3, as well as the MICAL-like proteins MICAL-L1 and MICAL-L2, but little is known of their function, and information comes almost exclusively from neural cells. In this study we show that in non-neural cells human MICALs are required for normal actin organization, and all three MICALs regulate actin stress fibers. Moreover, we provide evidence that the generation of reactive oxygen species by MICAL proteins is crucial for their actin-regulatory function. However, although MICAL1 is auto-inhibited by its C-terminal coiled-coil region, MICAL2 remains constitutively active and affects stress fibers. These data suggest differential but complementary roles for MICAL1 and MICAL2 in actin microfilament regulation.

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MICALs in control of the cytoskeleton, exocytosis, and cell death

Cited by 47 publications

References 92 publications

The Serine/Threonine Kinase Ndr2 Controls Integrin Trafficking and Integrin-Dependent Neurite Growth

The Serine/Threonine Kinase Ndr2 Controls Integrin Trafficking and Integrin-Dependent Neurite Growth

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

Differential regulation of actin microfilaments by human MICAL proteins

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