MICAL, a Novel CasL Interacting Molecule, Associates with Vimentin

Suzuki, Takahiro; Nakamoto, Tetsuya; Ogawa, Seishi; Seo, Sachiko; Matsumura, Tomoko; Tachibana, Kunihide; Morimoto, Chikao; Hirai, Hisamaru

doi:10.1074/jbc.m111842200

Cited by 136 publications

(171 citation statements)

References 55 publications

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“…The overall domain organization of mouse (and rat) MICALs is similar to that described for fly and human MICALs (Fig. 1A and not shown) (Suzuki et al, 2002;Terman et al, 2002;Weide et al, 2003). Both vertebrate and invertebrate MICALs contain a putative NH 2 -terminal monooxygenase domain of about 500 amino acids that can bind flavin-adenine dinucleotide (FAD), reduce NADPH, and which has a molecular structure identical to other monooxygenase domains.…”

Section: Resultsmentioning

confidence: 68%

“…Comparison of previously identified human MICAL sequences (Suzuki et al, 2002;Terman et al, 2002;Weide et al, 2003) with DNA sequence databanks led to the identification of three MICAL genes in mice and rats (MICAL-1, -2, and -3). The overall domain organization of mouse (and rat) MICALs is similar to that described for fly and human MICALs (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…In a search for plexin-interacting proteins in Drosophila, we identified Molecule interacting with CasL (MICAL; Suzuki et al, 2002) as a novel mediator of semaphorin signaling (Terman et al, 2002). MICALs comprise a small family of phylogenetically conserved cytosolic proteins that contain a putative NH 2 -terminal flavin-adenine dinucleotide (FAD)-binding monooxygenase domain.…”

Section: Introductionmentioning

confidence: 99%

“…Site-directed mutagenesis leading to alterations in amino acids in the D-MICAL monooxygenase region likely to be essential for monooxygenase function attenuates repulsive Sema1a signaling in vivo (Terman et al, 2002). In addition to D-MICAL, three human MICAL genes have been identified (MICAL-1, -2, and -3) (Suzuki et al, 2002;Terman et al, 2002;Weide et al, 2003). Expression analysis and yeast interaction experiments suggest that vertebrate MICALs function downstream of class 3 semaphorins (Sema3s) and their receptors, the vertebrate class A plexins (plexinAs) (Terman et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…In addition to a putative monooxygenase enzymatic domain, MICALs contain additional well-conserved domains known for interactions with actin, cytoskeletal adaptor proteins, and additional signaling molecules including coiled-coil, calponin homology, and LIM domains. To date, human and rodent MICALs have been shown to bind CasL, vimentin, rab1, and plexinAs (Fischer et al, 2005;Suzuki et al, 2002;Terman et al, 2002;Weide et al, 2003). The biological functions of vertebrate MICAL proteins, however, remain unknown.…”

Section: Introductionmentioning

confidence: 99%

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MICAL flavoprotein monooxygenases: Expression during neural development and following spinal cord injuries in the rat

Pasterkamp

Dai

Terman³

et al. 2006

Molecular and Cellular Neuroscience

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Section: Resultsmentioning

confidence: 68%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

MICAL flavoprotein monooxygenases: Expression during neural development and following spinal cord injuries in the rat

Pasterkamp

Dai

Terman³

et al. 2006

Molecular and Cellular Neuroscience

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Extracellular inhibitors, repellents, and semaphorin/plexin/MICAL‐mediated actin filament disassembly

2011

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Multiple extracellular signals have been identified that regulate actin dynamics within motile cells, but how these instructive cues present on the cell surface exert their precise effects on the internal actin cytoskeleton is still poorly understood. One particularly interesting class of these cues is a group of extracellular proteins that negatively alter the movement of cells and their processes. Over the years, these types of events have been described using a variety of terms and herein we provide an overview of inhibitory/repulsive cellular phenomena and highlight the largest known protein family of repulsive extracellular cues, the Semaphorins. Specifically, the Semaphorins (Semas) utilize Plexin cell-surface receptors to dramatically collapse the actin cytoskeleton and we summarize what is known of the direct molecular and biochemical mechanisms of Sema-triggered actin filament (F-actin) disassembly. We also discuss new observations from our lab that reveal that the multi-domain oxidoreductase (Redox) enzyme MICAL, an important mediator of Sema/Plexin repulsion, is a novel F-actin disassembly factor. Our results indicate that MICAL triggers Sema/Plexin-mediated reorganization of the F-actin cytoskeleton and suggest a role for specific Redox signaling events in regulating actin dynamics.

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Cytoskeletal protein vimentin interacts with and regulates peroxisome proliferator‐activated receptor gamma via a proteasomal degradation process

Tsai

Chang

et al. 2013

J of Cellular Biochemistry

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Peroxisome proliferators-activated receptor gamma (PPARγ) receptor is a transcription factor that is located in and functions primarily in the nucleus. PPARγ is exported from the nucleus upon mitogen and ligand stimulation under certain circumstances. However, a cytoplasmic PPARγ interacting protein and its function have not been previously identified. Here, we report for the first time that cytosolic PPARγ interacts directly with cytoskeletal vimentin. We performed PPARγ immunoprecipitation followed by mass spectrometry to identify the vimentin-PPARγ complex. This interaction was confirmed by reciprocal vimentin and PPARγ immunoprecipitation and co-immunofluorescence examination. We demonstrated that PPARγ colocalized with vimentin in certain organelles that is golgi, mitochondria, and endoplasmic reticulum. In cells depleted of vimentin, PPARγ was ubiquitinated and targeted to a proteasomal degradation pathway. Together, these findings indicate a direct interaction of PPARγ with vimentin in the cytosolic compartment, in which vimentin appears to play a role in regulating the turnover rate of PPARγ, which may further regulate genomic or non-genomic activities through the regulation of PPARγ protein degradation.

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MICAL, a Novel CasL Interacting Molecule, Associates with Vimentin

Cited by 136 publications

References 55 publications

MICAL flavoprotein monooxygenases: Expression during neural development and following spinal cord injuries in the rat

MICAL flavoprotein monooxygenases: Expression during neural development and following spinal cord injuries in the rat

Extracellular inhibitors, repellents, and semaphorin/plexin/MICAL‐mediated actin filament disassembly

Cytoskeletal protein vimentin interacts with and regulates peroxisome proliferator‐activated receptor gamma via a proteasomal degradation process

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