Emerging roles of MICAL family proteins – from actin oxidation to membrane trafficking during cytokinesis

Frémont, Stéphane; Romet-Lemonne, Guillaume; Houdusse, Anne; Échard, Arnaud

doi:10.1242/jcs.202028

Cited by 78 publications

(70 citation statements)

References 100 publications

(162 reference statements)

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“…This oxidation appears to play a key role in the regulation of actin depolymerization and also potentially membrane trafficking (see Refs. 200 and Fremont et al (201). The detection of methionine sulfoxide may therefore not always be a marker of diffusible reactive oxidant species.…”

Section: Detection and Quantification Of Productsmentioning

confidence: 98%

Detection, identification, and quantification of oxidative protein modifications

Hawkins

Davies

2019

Journal of Biological Chemistry

309

209

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Edited by Ruma Banerjee Exposure of biological molecules to oxidants is inevitable and therefore commonplace. Oxidative stress in cells arises from both external agents and endogenous processes that generate reactive species, either purposely (e.g. during pathogen killing or enzymatic reactions) or accidentally (e.g. exposure to radiation, pollutants, drugs, or chemicals). As proteins are highly abundant and react rapidly with many oxidants, they are highly susceptible to, and major targets of, oxidative damage. This can result in changes to protein structure, function, and turnover and to loss or (occasional) gain of activity. Accumulation of oxidatively-modified proteins, due to either increased generation or decreased removal, has been associated with both aging and multiple diseases. Different oxidants generate a broad, and sometimes characteristic, spectrum of post-translational modifications. The kinetics (rates) of damage formation also vary dramatically. There is a pressing need for reliable and robust methods that can detect, identify, and quantify the products formed on amino acids, peptides, and proteins, especially in complex systems. This review summarizes several advances in our understanding of this complex chemistry and highlights methods that are available to detect oxidative modifications-at the amino acid, peptide, or protein level-and their nature, quantity, and position within a peptide sequence. Although considerable progress has been made in the development and application of new techniques, it is clear that further development is required to fully assess the relative importance of protein oxidation and to determine whether an oxidation is a cause, or merely a consequence, of injurious processes.

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Section: Detection and Quantification Of Productsmentioning

confidence: 98%

Detection, identification, and quantification of oxidative protein modifications

Hawkins

Davies

2019

Journal of Biological Chemistry

309

209

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“…Finally, another member of the MICAL family [91], MICAL3, is involved in the tethering of Rab8 vesicles at the midbody before fusion with the plasma membrane [92]. Rab8 endosomes within bridges are distinct and arrive before FIP3 endosomes [46].…”

Section: Docking Vesicles By Multiple Mechanismsmentioning

confidence: 99%

Membrane Traffic in the Late Steps of Cytokinesis

2018

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Cells don't simply separate at cytokinesis. While furrow contraction critically relies on myosin-II and F-actin, post-furrowing steps are less understood but involve the constriction of ESCRT-III polymer-dependent helices on the side of the midbody, which likely drive final abscission. The first evidence that animal cell cytokinesis requires membrane traffic, as in plant cells, was provided about 15 years ago. Since then, it has become increasingly clear that fusion of vesicles to the cytokinetic furrow is essential in large embryonic cells, and that membrane traffic within the intercellular bridge is crucial for its stability and successful abscission in all animal cells. Here, we review our current knowledge of the secretory and endocytic recycling pathways involved in cytokinesis, and how vesicles defined by specific Rab and Arf GTPases are targeted and fused to the membrane of the intercellular bridge thanks to different molecular motors, tethering complexes and SNARE machineries. At the functional level, we will describe how membrane traffic can remodel both phosphoinositide lipids and promote F-actin clearance necessary for ESCRT-III-dependent abscission, and identify key unanswered questions in the field. We will finally review recent evidence showing a tight coupling between membrane traffic and cytokinesis in complex processes, such as during the establishment of de novo apico-basal polarity.

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“…Of note, OCRL traffics in and out of the cytokinetic bridge on Rab35‐positive vesicles . Another Rab35 effector, MICAL1, which belongs to an emerging class of oxidation‐reduction enzymes that depolymerize filamentous actin (F‐actin) through selective oxidation, facilitates ESCRT‐III recruitment at cytokinetic bridges and thus abscission . Both OCRL and MICAL1 localize to cytokinetic bridges in a Rab35‐dependent manner, and their depletion causes the accumulation of F‐actin at this location .…”

Section: Rab35 In Membrane Trafficking and Cell Divisionmentioning

confidence: 99%

“…In parallel to phosphoinositide regulation, Rab35 controls recycling of cargoes from ADP‐ribosylation factor 6 (ARF6)‐positive endosomes back to the plasma membrane through the recruitment of 2 additional effectors: the ARF6‐GAP ACAP2/CentaurinB2 and MICAL‐L1, a scaffolding protein that, contrary to MICAL1 described above, has no redox activity . For detailed reviews on ARF proteins and cancer, please refer to refs …”

Section: Rab35 In Membrane Trafficking and Cell Signalingmentioning

confidence: 99%

Rab35 GTPase and cancer: Linking membrane trafficking to tumorigenesis

Shaughnessy

Échard

2018

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Rab35 is a small GTPase that is involved in many cellular processes, including membrane trafficking, cell polarity, lipid homeostasis, immunity, phagocytosis and cytokinesis. Recent studies showed that activating mutations confer Rab35 with oncogenic properties. Conversely, downregulation of Rab35 inverts apico-basal cell polarity and promotes cell migration. Here we review Rab35's known functions in membrane trafficking and signaling, cell division and cell migration in cancer cells and discuss the importance of Rab35-dependent membrane trafficking in cancer progression.

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Emerging roles of MICAL family proteins – from actin oxidation to membrane trafficking during cytokinesis

Cited by 78 publications

References 100 publications

Detection, identification, and quantification of oxidative protein modifications

Detection, identification, and quantification of oxidative protein modifications

Membrane Traffic in the Late Steps of Cytokinesis

Rab35 GTPase and cancer: Linking membrane trafficking to tumorigenesis

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