Dual roles for the <i>Drosophila</i> PI 4-kinase Four wheel drive in localizing Rab11 during cytokinesis

Polevoy, Gordon; Wei, Ho-Chun; Wong, Raymond; Szentpétery, Zsófia; Kim, Yeun Ju; Goldbach, Philip; Steinbach, Sarah K.; Balla, Tamás; Brill, Julie A.

doi:10.1083/jcb.200908107

Cited by 119 publications

(179 citation statements)

References 73 publications

Supporting

Mentioning

172

Contrasting

Order By: Relevance

“…Previous data from D. melanogaster and yeast corroborate our data: Exocytic traffic to the midbody in cytokinesis requires PI(4)P on Rab11-positive recycling endosomes, shown in D.melanogaster (Polevoy, Wei et al 2009). In yeast, trafficking from the TGN en route to the PM is regulated by PI(4)P levels on Rab11-positive secretory vesicles (Mizuno-Yamasaki, Medkova et al 2010).…”

Section: Pi Conversion In Endosomal Exocytosis Parallels Switching Ofsupporting

confidence: 90%

“…In addition, PI4K3α maintains the PM pool of PI(4)P (Balla, Tuymetova et al 2005) and PI(4,5)P 2 (Bojjireddy, Botyanszki et al 2014). At the Golgi complex, PI(4)P-production by PI4K3β and its association with Rab11 are required for secretory membrane traffic and during cytokinesis (Polevoy, Wei et al 2009). In addition PI4K3β has been found in the nucleus with so far unknown function.…”

Section: Other Myotubularin Family Members Contribute To Endosomal Pimentioning

confidence: 99%

See 1 more Smart Citation

A phosphoinositide conversion mechanism for exit from endosomes

Ketel¹,

Krauß²,

Nicot³

et al. 2016

Nature

161

177

View full text Add to dashboard Cite

I owe special thanks to Marnix Wieffer and Michael Krauß, who spent a lot of time helping me to get started in the lab, to overcome numerous experimental problem, I was not sure how to deal with, and frequently joined in discussions about my project with excellent advice. I am really grateful for your experimental support, Michael, and the time you invested in the project during our paper revision.Further, I would like to thank Jocelyn Laporte and his group, especially Anne-Sophie Nicot, at the IGBMC in Strasbourg for their support and a very fruitful collaboration, and Carsten Schultz and his group at the EMBL in Heidelberg for their support and constant supply with PIP/AMs. I owe special thanks to Dmytro Puchkov for the ultrastructural analysis and Eberhard Krause for mass spectrometry done within this project. I also need to acknowledge Markus Wenk and Federico Torta at the Singapore Lipidomics Incubator for joining the project at a very late stage, when we urgently needed help from lipidomics specialists. It was a pity that experiments did not work out as planned.I would further like to express my gratitude to two very skilled technicians in the AG Haucke lab: Silke Zillmann and Delia Löwe. Without your help it would have been impossible to achieve so much within the limited amount of time I had during the paper revision. by VPS34-IN1 treatment................................................... 52 2.3.11 Fluorescence microscopy................................................................................. 53 2.3.12 Flow cytometry............................................................................................ III SummaryPhosphoinositides (PIs) are a minor class of short-lived phospholipids that serve as crucial signposts of membrane identity. Thereby, PIs full fill important functions in cell signaling and membrane transport. PI 4-phosphates such as phosphatitylinositol-4-phosphate (PI(4)P) and phosphatitylinositol-4,5-bisphosphate (PI(4,5)P 2 ) are enriched at the plasma membrane (PM), on secretory organelles and lysosomes, while PI 3-phosphates, i.e.phosphatitylinositol-3-phosphate (PI(3)P), are a hallmark of the endosomal system.Directional transport between these compartments, thus, requires regulated PI conversion.However, PI conversion in exit from PI(3)P-enriched endosomes en route to the PI(4)P-and PI(4,5)P 2 -positive PM in endosomal recycling remained unknown.Here, we report that cargo exit from endosomes requires removal of PI(3)P by the PI(3)P 3-phosphatase myotubularin 1 (MTM1), and concomitant PI(4)P synthesis by PI 4-kinase type II α (PI4K2α). Loss of MTM1 causes endosomal accumulation of PI(3)P and PI(3)P effector proteins, i.e. sorting nexins, Kif16b-mediated outward traffic of PI(3)P containing endosomes and sub-plasmalemmal accumulation of exocytosis-deficient endosomes. As PI4K2α associates with MTM1 and thereby facilitates membrane recruitment of MTM1, these phenotypic changes are mimicked by loss of PI4K2α. The conversion of PI(3)P-to-PI(4)P is paralleled by a switch i...

show abstract

Section: Pi Conversion In Endosomal Exocytosis Parallels Switching Ofsupporting

confidence: 90%

Section: Other Myotubularin Family Members Contribute To Endosomal Pimentioning

confidence: 99%

A phosphoinositide conversion mechanism for exit from endosomes

Ketel¹,

Krauß²,

Nicot³

et al. 2016

Nature

161

177

View full text Add to dashboard Cite

show abstract

“…Similarly, PtdIns4P can be generated by the activity of PtdIns 4-kinases (PI4Ks) (Figure 1) in mammals and four wheel drive (fwd) in Drosophila, a type III PI4K that uses PtdIns as a substrate (Brill et al, 2000;Polevoy et al, 2009).…”

Section: Ptdins Production and Function During Cytokinesismentioning

confidence: 99%

“…One possible function of the vesicles containing PtdIns4P might be the delivery of this PtdIns during late cytokinetic furrowing, where it could serve as a precursor for the PtdIns(4,5)P2 synthesis and thus promoting furrow stability (Polevoy et al, 2009). Intriguingly, genetic analysis indicates that Fwd contributes to cytokinesis both in a kinase-dependent and in a kinase-independent manner (Polevoy et al, 2009). This is possibly due to the fact that Drosophila Fwd and mammalian PI4Kβ have non enzymatic function and directly recruit Rab11 on Golgi membranes.…”

Section: Ptdins Production and Function During Cytokinesismentioning

confidence: 99%

“…This is possibly due to the fact that Drosophila Fwd and mammalian PI4Kβ have non enzymatic function and directly recruit Rab11 on Golgi membranes. Given that Rab11 can bind simultaneously to effectors and to PI4K (Burke et al, 2014) and function downstream to Fwd in Drosophila (Polevoy et al, 2009), one key function of PI4K in abscission might be to regulate Rab11 association with membranes directed to the furrow during cytokinesis. Rab11 has been shown to regulate F-actin organization and remodelling at the intracellular bridge during cytokinesis (Cao et al, 2008;Hickson et al, 2003;Schiel et al, 2012).…”

Section: Ptdins Production and Function During Cytokinesismentioning

confidence: 99%

See 1 more Smart Citation

Cytokinetic Abscission: Phosphoinositides and ESCRTs Direct the Final Cut

Gulluni

Martini

Hirsch

2017

J of Cellular Biochemistry

View full text Add to dashboard Cite

Cytokinetic abscission involves the fine and regulated recruitment of membrane remodeling proteins that participate in the abscission of the intracellular bridge that connects the two dividing cells. This essential process is mediated by the concomitant activity of the endosomal sorting complex required for transport (ESCRT) and the vesicular trafficking directed to the midbody.Phosphoinositides (PtdIns), produced at plasma membrane and endosomes, act as molecular intermediates by recruiting effector proteins involved in multiple cellular processes, such as intracellular signalling, endo-and exo-cytosis and membrane remodelling events. Emerging evidences suggest that PtdIns have an active role in recruiting key elements that control the stability and the remodelling of the cytoskeleton from the furrow ingression to the abscission, at the end of cytokinesis. Accordingly, a possible concomitant and coordinated activity between PtdIns production and ESCRT machinery assembly could also exist and recent findings are pointing the attention on poorly understood ESCRT subunits potentially able to associate with PtdIns rich membranes. Although further studies are required to link PtdIns to ESCRT machinery during abscission, this might represent a promising field of study.

show abstract