Linking cytoplasmic dynein and transport of Rab8 vesicles to the midbody during cytokinesis by the doublecortin domain-containing 5 protein

Kaplan, Ariel; Reiner, Orly

doi:10.1242/jcs.085407

Cited by 38 publications

(29 citation statements)

References 75 publications

(72 reference statements)

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“…Additionally, recently published work also suggested that Rab5, Rab6, Rab8a, Rab21 and Rab24 may also play a role in cytokineis, although their exact function remains to be fully understood. [47][48][49][50][51] What, if any, function do these Rab GTPases play during cytokinesis remains to be determined and will require further studies. Additionally, very little is known about the involvement of Rabs and endocytic membrane transport in regulating specialized and assymetric types of cytokinesis and abscission.…”

Section: Discussionmentioning

confidence: 99%

Rab GTPases and cell division

Gibieža

Prekeris

2017

Small GTPases

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Cytokinesis is a complex cellular process that leads to a physical separation of two daughter cells. The key to a successful cytokinesis is a coordinated reorganization of cellular cytoskeleton and membrane trafficking pathways. Consequently, Rab GTPases recently emerged as major regulators of cellular division. Rabs belong to a superfamily of small monomeric GTPases that regulate a diverse array of cellular functions. Rabs in particular are well-established regulators of membrane transport and have been shown to mediate several membrane transport steps including vesicle formation, molecular motor-dependent vesicle transport and targeting of transport vesicles and organelles to their correct destinations. Significantly, several Rab GTPases also have been shown to function in regulating cell division. In this review, we discuss latest findings about the function of Rabs and polarized membrane transport during different steps of cytokinesis as well as during the final stage of cell division known as abscission.

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Section: Discussionmentioning

confidence: 99%

Rab GTPases and cell division

Gibieža

Prekeris

2017

Small GTPases

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“…This protein has been demonstrated to direct polarized trafficking events during ciliogenesis, neuronal development, regulated secretion and cytokinesis (Yoshimura et al, 2007;Nachury et al, 2007;Huber et al, 1995;Chen et al, 2001;Kaplan and Reiner, 2011), possibly through the ability to reorganize actin and microtubules (Peränen et al, 1996). Defects in Rab8 function have been implicated in trafficking diseases, including retinal degeneration, cell polarity defects and irregular tissue formation (Moritz et al, 2001;Satoh et al, 2007;Huber et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Rab8 directs furrow ingression and membrane addition during epithelial formation in Drosophila melanogaster

et al. 2016

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One of the most fundamental changes in cell morphology is the ingression of a plasma membrane furrow. The Drosophila embryo undergoes several cycles of rapid furrow ingression during early development that culminate in the formation of an epithelial sheet. Previous studies have demonstrated the requirement for intracellular trafficking pathways in furrow ingression; however, the pathways that link compartmental behaviors with cortical furrow ingression events are unclear. Here, we show that Rab8 has striking dynamic behaviors in vivo. As furrows ingress, cytoplasmic Rab8 puncta are depleted and Rab8 accumulates at the plasma membrane in a location that coincides with known regions of directed membrane addition. We additionally use CRISPR/Cas9 technology to N-terminally tag Rab8, which is then used to address endogenous localization and function. Endogenous Rab8 displays partial coincidence with Rab11 and the Golgi, and this colocalization is enriched during the fast phase of cellularization. When Rab8 function is disrupted, furrow formation in the early embryo is completely abolished. We also demonstrate that Rab8 behaviors require the function of the exocyst complex subunit Sec5 as well as the recycling endosome protein Rab11. Active, GTPlocked Rab8 is primarily associated with dynamic membrane compartments and the plasma membrane, whereas GDP-locked Rab8 forms large cytoplasmic aggregates. These studies suggest a model in which active Rab8 populations direct furrow ingression by guiding the targeted delivery of cytoplasmic membrane stores to the cell surface through interactions with the exocyst tethering complex.

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“…During cytokinesis, MICAL3 directly interacts with the centralspindlin component MKLP1 (also known as KIF23) and recruits the adaptor protein ELKS (also known as ERC1), which tethers Rab8A-positive vesicles to the midbody . Importantly, Rab8A vesicles are known to transport important molecules, which are yet to be identified, that promote late cytokinetic steps (Guizetti et al, 2011;Kaplan and Reiner, 2011;Schiel et al, 2012). As a consequence, the depletion of either ELKS or Rab8A leads to abscission defects.…”

Section: Activation Of Mical1mentioning

confidence: 99%

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

Frémont

Romet-Lemonne

Houdusse

et al. 2017

Journal of Cell Science

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Cytokinetic abscission is the terminal step of cell division, leading to the physical separation of the two daughter cells. The exact mechanism mediating the final scission of the intercellular bridge connecting the dividing cells is not fully understood, but requires the local constriction of endosomal sorting complex required for transport (ESCRT)-III-dependent helices, as well as remodelling of lipids and the cytoskeleton at the site of abscission. In particular, microtubules and actin filaments must be locally disassembled for successful abscission. However, the mechanism that actively removes actin during abscission is poorly understood. In this Commentary, we will focus on the latest findings regarding the emerging role of the MICAL family of oxidoreductases in F-actin disassembly and describe how Rab GTPases regulate their enzymatic activity. We will also discuss the recently reported role of MICAL1 in controlling F-actin clearance in the ESCRT-III-mediated step of cytokinetic abscission. In addition, we will highlight how two other members of the MICAL family (MICAL3 and MICAL-L1) contribute to cytokinesis by regulating membrane trafficking. Taken together, these findings establish the MICAL family as a key regulator of actin cytoskeleton dynamics and membrane trafficking during cell division.

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Linking cytoplasmic dynein and transport of Rab8 vesicles to the midbody during cytokinesis by the doublecortin domain-containing 5 protein

Cited by 38 publications

References 75 publications

Rab GTPases and cell division

Rab GTPases and cell division

Rab8 directs furrow ingression and membrane addition during epithelial formation in Drosophila melanogaster

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

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