The Diversification of the LIM Superclass at the Base of the Metazoa Increased Subcellular Complexity and Promoted Multicellular Specialization

Koch, Bernard; Ryan, Joseph F.; Baxevanis, Andreas D.

doi:10.1371/journal.pone.0033261

Cited by 53 publications

(73 citation statements)

References 104 publications

(157 reference statements)

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“…Many known LIM proteins have been shown to bind F-actin or actin-binding proteins (Khurana et al, 2002), but none have been described that contain a VIN domain. T. trahens VIN 2 appears to be a novel VIN-LIM-containing protein that represents a class of eukaryotic LIM proteins that were not described previously (Koch et al, 2012). The inclusion of a transmembrane domain in A. castellani VIN 2 is also novel – no other described VIN protein has been observed to have a transmembrane domain.…”

Section: Genomic Analysis Of CCC Evolutionmentioning

confidence: 84%

The Evolutionary Origin of Epithelial Cell–Cell Adhesion Mechanisms

Miller

Clarke

Weis

et al. 2013

Current Topics in Membranes

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SUMMARY A simple epithelium forms a barrier between the outside and the inside of an organism, and is the first organized multicellular tissue found in evolution. We examine the relationship between the evolution of epithelia and specialized cell-cell adhesion proteins comprising the classical cadherin/β-catenin/α-catenin complex (CCC). A review of the divergent functional properties of the CCC in metazoans and non-metazoans, and an updated phylogenetic coverage of the CCC using recent genomic data reveal: 1) The core CCC likely originated before the last common ancestor of unikonts and their closest bikont sister taxa. 2) Formation of the CCC may have constrained sequence evolution of the classical cadherin cytoplasmic domain and β-catenin in metazoa. 3) The α-catenin binding domain in β-catenin appears to be the favored mutation site for disrupting β-catenin function in the CCC. 4) The ancestral function of the α/β-catenin heterodimer appears to be an actin-binding module. In some metazoan groups, more complex functions of α-catenin were gained by sequence divergence in the non-actin binding (N-, M-) domains. 5) Allosteric regulation of α-catenin, rather than loss of function mutations, may have evolved for more complex regulation of the actin cytoskeleton.

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Section: Genomic Analysis Of CCC Evolutionmentioning

confidence: 84%

The Evolutionary Origin of Epithelial Cell–Cell Adhesion Mechanisms

Miller

Clarke

Weis

et al. 2013

Current Topics in Membranes

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“…The LIM superclass of genes can be classified into 15 classes: ABLIM, CRP, ENIGMA, EPLIN, FHL, LASP, LHX, LMO, LIMK, LMO7, MICAL, PXN, PINCH, TES and ZYX103940. Some LIM genes are expressed in a cell- and tissue-specific manner.…”

Section: Discussionmentioning

confidence: 99%

A signature motif in LIM proteins mediates binding to checkpoint proteins and increases tumour radiosensitivity

Zhang²,

Liang³

et al. 2017

Nat Commun

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Tumour radiotherapy resistance involves the cell cycle pathway. CDC25 phosphatases are key cell cycle regulators. However, how CDC25 activity is precisely controlled remains largely unknown. Here, we show that LIM domain-containing proteins, such as FHL1, increase inhibitory CDC25 phosphorylation by forming a complex with CHK2 and CDC25, and sequester CDC25 in the cytoplasm by forming another complex with 14-3-3 and CDC25, resulting in increased radioresistance in cancer cells. FHL1 expression, induced by ionizing irradiation in a SP1- and MLL1-dependent manner, positively correlates with radioresistance in cancer patients. We identify a cell-penetrating 11 amino-acid motif within LIM domains (eLIM) that is sufficient for binding CHK2 and CDC25, reducing the CHK2–CDC25 and CDC25–14-3-3 interaction and enhancing CDC25 activity and cancer radiosensitivity accompanied by mitotic catastrophe and apoptosis. Our results provide novel insight into molecular mechanisms underlying CDC25 activity regulation. LIM protein inhibition or use of eLIM may be new strategies for improving tumour radiosensitivity.

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“…LIM is an ancient eukaryotic protein domain that originated prior to the last common ancestor of plants, fungi, amoebae, and animals 154 . Its name is an acronym of the first three genes in which it was identified: Lin-11 , Isl1 and Mec-3 155 .…”

Section: Micalmentioning

confidence: 99%

Regulated methionine oxidation by monooxygenases

Manta

Gladyshev

2017

Free Radical Biology and Medicine

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Protein function can be regulated via post-translational modifications by numerous enzymatic and non-enzymatic mechanisms, including oxidation of cysteine and methionine residues. Redox-dependent regulatory mechanisms have been identified for nearly every cellular process, but the major paradigm has been that cellular components are oxidized (damaged) by reactive oxygen species (ROS) in a relatively unspecific way, and then reduced (repaired) by designated reductases. While this scheme may work with cysteine, it cannot be ascribed to other residues, such as methionine, whose reaction with ROS is too slow to be biologically relevant. However, methionine is clearly oxidized in vivo and enzymes for its stereoselective reduction are present in all three domains of life. Here, we revisit the chemistry and biology of methionine oxidation, with emphasis on its generation by enzymes from the monooxygenase family. Particular attention is placed on MICALs, a recently discovered family of proteins that harbor an unusual flavin-monooxygenase domain with an NADPH-dependent methionine sulfoxidase activity. Based on the structural and kinetic information we provide a rational framework to explain MICAL mechanism, inhibition, and regulation. Methionine residues that are targeted by MICALs are reduced back by methionine sulfoxide reductases, suggesting that reversible methionine oxidation may be a general mechanism analogous to the regulation by phosphorylation by kinases/phosphatases. The identification of new enzymes that catalyze the oxidation of methionine will open a new area of research at the forefront of redox signaling.

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The Diversification of the LIM Superclass at the Base of the Metazoa Increased Subcellular Complexity and Promoted Multicellular Specialization

Cited by 53 publications

References 104 publications

The Evolutionary Origin of Epithelial Cell–Cell Adhesion Mechanisms

The Evolutionary Origin of Epithelial Cell–Cell Adhesion Mechanisms

A signature motif in LIM proteins mediates binding to checkpoint proteins and increases tumour radiosensitivity

Regulated methionine oxidation by monooxygenases

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