We are analyzing https://link.springer.com/article/10.1007/s00018-011-0787-2.

Title:
MICALs in control of the cytoskeleton, exocytosis, and cell death | Cellular and Molecular Life Sciences
Description:
MICALs form an evolutionary conserved family of multidomain signal transduction proteins characterized by a flavoprotein monooxygenase domain. MICALs are being implicated in the regulation of an increasing number of molecular and cellular processes including cytoskeletal dynamics and intracellular trafficking. Intriguingly, some of these effects are dependent on the MICAL monooxygenase enzyme and redox signaling, while other functions rely on other parts of the MICAL protein. Recent breakthroughs in our understanding of MICAL signaling identify the ability of MICALs to bind and directly modify the actin cytoskeleton, link MICALs to the docking and fusion of exocytotic vesicles, and uncover MICALs as anti-apoptotic proteins. These discoveries could lead to therapeutic advances in neural regeneration, cancer, and other diseases.
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Keywords {🔍}

mical, article, pubmed, google, scholar, cas, proteins, domain, micals, cell, protein, signaling, axon, crmp, ndr, biol, actin, drosophila, function, guidance, binding, fig, rab, mst, kinases, family, region, cytoskeleton, lim, regulation, role, domains, interaction, development, cterminal, apoptosis, semaa, kinase, cellular, functions, factin, activity, structure, cells, growth, bind, required, dendritic, expression, plexina,

Topics {✒️}

pro-pro-lys-pro-pro article download pdf tricornered-kinase/furry signaling pathway ecdysone-induced transcription factor c-terminal coiled-coil motifs plexin-mediated axonal repulsion boundary cap cells glycogen synthase kinase-3β gsk-3β-mediated crmp-2 phosphorylation vesicle-docking protein complexes glutathione/glutaredoxin reductase system glutamic acid-rich motif proline-rich region close purified c-terminal region n-terminal flavoprotein monooxygenase c-terminal hydrophobic motif plexa-deficient flies suggesting glutamic acid-repeat region junctional rab13-binding protein serine/threonine kinase ndr2 n-terminal mo domain semaphorin signalling ll5β/elks-positive sites sema/plexina2/mical-3 pathway protein–protein interaction modules protein–protein interaction module n-terminal enzymatic region neural crest-derived cells controlling pro-apoptotic signaling multidomain flavoenzyme-signaling molecule conserved n-terminal region full-length mical genes mst-ndr kinase signaling adapter protein cas actin-cross-linking proteins large active-site cavity sema-1a ligand binding p130 cas family facilitate f-actin binding ndr-dependent cellular processes vesicle-docking protein complex protein–protein interaction domains reduces ndr activity proline-rich regions extracellular environment tnf-α induce activation contraction responses observed semaphorin/plexin signaling rab family small c-terminal regions

Questions {❓}

Fischer J, Weide T, Barnekow A (2005) The MICAL proteins and Rab1: a possible link to the cytoskeleton?
Schmidt ER, Pasterkamp RJ, van den Berg LH (2009) Axon guidance proteins: novel therapeutic targets for ALS?

Schema {🗺️}

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         headline:MICALs in control of the cytoskeleton, exocytosis, and cell death
         description:MICALs form an evolutionary conserved family of multidomain signal transduction proteins characterized by a flavoprotein monooxygenase domain. MICALs are being implicated in the regulation of an increasing number of molecular and cellular processes including cytoskeletal dynamics and intracellular trafficking. Intriguingly, some of these effects are dependent on the MICAL monooxygenase enzyme and redox signaling, while other functions rely on other parts of the MICAL protein. Recent breakthroughs in our understanding of MICAL signaling identify the ability of MICALs to bind and directly modify the actin cytoskeleton, link MICALs to the docking and fusion of exocytotic vesicles, and uncover MICALs as anti-apoptotic proteins. These discoveries could lead to therapeutic advances in neural regeneration, cancer, and other diseases.
         datePublished:2011-08-06T00:00:00Z
         dateModified:2011-08-06T00:00:00Z
         pageStart:4033
         pageEnd:4044
         license:https://creativecommons.org/licenses/by-nc/2.0
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         keywords:
            Apoptosis
            Axon guidance
            Cytoskeleton
            Exocytosis
            NDR kinase
            Plexin
            Rab GTPase
            Semaphorin
            Cell Biology
            Biomedicine
            general
            Life Sciences
            Biochemistry
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ScholarlyArticle:
      headline:MICALs in control of the cytoskeleton, exocytosis, and cell death
      description:MICALs form an evolutionary conserved family of multidomain signal transduction proteins characterized by a flavoprotein monooxygenase domain. MICALs are being implicated in the regulation of an increasing number of molecular and cellular processes including cytoskeletal dynamics and intracellular trafficking. Intriguingly, some of these effects are dependent on the MICAL monooxygenase enzyme and redox signaling, while other functions rely on other parts of the MICAL protein. Recent breakthroughs in our understanding of MICAL signaling identify the ability of MICALs to bind and directly modify the actin cytoskeleton, link MICALs to the docking and fusion of exocytotic vesicles, and uncover MICALs as anti-apoptotic proteins. These discoveries could lead to therapeutic advances in neural regeneration, cancer, and other diseases.
      datePublished:2011-08-06T00:00:00Z
      dateModified:2011-08-06T00:00:00Z
      pageStart:4033
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      license:https://creativecommons.org/licenses/by-nc/2.0
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      keywords:
         Apoptosis
         Axon guidance
         Cytoskeleton
         Exocytosis
         NDR kinase
         Plexin
         Rab GTPase
         Semaphorin
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
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         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00018-011-0787-2/MediaObjects/18_2011_787_Fig1_HTML.gif
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            name:University Medical Center Utrecht
            address:
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               type:PostalAddress
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      affiliation:
            name:University Medical Center Utrecht
            address:
               name:Department of Neuroscience and Pharmacology, University Medical Center Utrecht, Utrecht, The Netherlands
               type:PostalAddress
            type:Organization
      name:R. Jeroen Pasterkamp
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            name:University Medical Center Utrecht
            address:
               name:Department of Neuroscience and Pharmacology, University Medical Center Utrecht, Utrecht, The Netherlands
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      name:Department of Neuroscience and Pharmacology, University Medical Center Utrecht, Utrecht, The Netherlands
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      name:Department of Neuroscience and Pharmacology, University Medical Center Utrecht, Utrecht, The Netherlands

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