Linking up at the BAR: Oligomerization and F-BAR protein function

McDonald, Nathan A.; Gould, Kathleen L.

doi:10.1080/15384101.2016.1190893

Cited by 29 publications

(37 citation statements)

References 109 publications

(154 reference statements)

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“…Unlike Hof1 in budding yeast or Cdc15 in the fission yeast S. pombe [33, 46], many F-BAR domain-containing proteins can generate membrane curvatures by forming helical filaments via lateral as well as end-to-end associations [21]. The F-BAR proteins usually link cellular membranes to the actin cytoskeleton and/or cellular signaling via other domains such as the SH3 and GTPase-activating domains (GAPs) for Rho GTPases and function in a number of cellular processes such as endocytosis, cell migration, and cytokinesis [22, 46]. Very few protein partners of F-BAR domains have been identified and characterized, with the exceptions that the F-BAR of Cdc15 in fission yeast interacts with the formin Cdc12 to fine-tune AMR assembly [47], and that the F-BAR of PSTPIP1 in mammalian cells interacts with pyrin to regulate inflammatory responses [48].…”

Section: Resultsmentioning

confidence: 99%

“…In addition, Hof1 is required for rapid accumulation as well as efficient removal of Chs4 at the division site. This study uncovers a mechanism by which Hof1 controls timely activation of Chs3 during cytokinesis, and defines a novel interaction and function for the conserved F-BAR domain and SLR that are otherwise known for their abilities to bind membrane lipids [21, 22] and scaffold protein complex formation [23]. …”

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confidence: 99%

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Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis

Schreiter

Okada

et al. 2017

Current Biology

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SUMMARY Localized extracellular matrix (ECM) remodeling is thought to stabilize the cleavage furrow and maintain cell shape during cytokinesis [1–14]. This remodeling is spatiotemporally coordinated with a cytoskeletal structure pertaining to a kingdom of life, for example, the FtsZ ring in bacteria [15], the phragmoplast in plants [16], and the actomyosin ring in fungi and animals [17, 18]. While the cytoskeletal structures have been analyzed extensively, the mechanisms of ECM remodeling remain poorly understood. In the budding yeast Saccharomyces cerevisiae, the ECM remodeling refers to sequential formations of the primary and secondary septa that are catalyzed by chitin synthase-II (Chs2) and chitin synthase-III (the catalytic subunit Chs3 and its activator Chs4), respectively [18, 19]. Surprisingly, both Chs2 and Chs3 are delivered to the division site at the onset of cytokinesis [6, 20]. What keeps Chs3 inactive until secondary septum formation remains unknown. Here, we show that Hof1 binds to the Sel1-like repeats (SLR) of Chs4 via its F-BAR domain, and inhibits Chs3-mediated chitin synthesis during cytokinesis. In addition, Hof1 is required for rapid accumulation as well as efficient removal of Chs4 at the division site. This study uncovers a mechanism by which Hof1 controls timely activation of Chs3 during cytokinesis, and defines a novel interaction and function for the conserved F-BAR domain and SLR that are otherwise known for their abilities to bind membrane lipids [21, 22] and scaffold protein complex formation [23].

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis

Schreiter

Okada

et al. 2017

Current Biology

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“…Dynamin 2 mediates fission during endocytosis, converting clathrin-coated pits into endosomes (Antonny et al, 2016). Alternatively, Dynamin 2 might promote membrane remodelling by interacting with proteins with Bin-amphiphysin-rvs (BAR) domains (Daumke, Roux, & Haucke, 2014;McDonald & Gould, 2016). Alternatively, Dynamin 2 might promote membrane remodelling by interacting with proteins with Bin-amphiphysin-rvs (BAR) domains (Daumke, Roux, & Haucke, 2014;McDonald & Gould, 2016).…”

Section: Hgf Promotes Exocytosis and Internalisation Of Particlesmentioning

confidence: 99%

“…Although it is formally possible that Dynamin 2 plays an analogous role in in InlB-dependent entry, it is unclear if the GTPase could mediate scission of phagosomes, which are more than 10 times the size of conventional endosomes (Conner & Schmid, 2003). Alternatively, Dynamin 2 might promote membrane remodelling by interacting with proteins with Bin-amphiphysin-rvs (BAR) domains (Daumke, Roux, & Haucke, 2014;McDonald & Gould, 2016). BAR domains have curved surfaces capable of deforming membranes.…”

Section: Hgf Promotes Exocytosis and Internalisation Of Particlesmentioning

confidence: 99%

A role for host cell exocytosis in InlB-mediated internalisation ofListeria monocytogenes

Ngo

Bhalla

Chen

et al. 2017

Cellular Microbiology

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The bacterial surface protein InlB mediates internalisation of Listeria monocytogenes into human cells through interaction with the host receptor tyrosine kinase, Met. InlB-mediated entry requires localised polymerisation of the host actin cytoskeleton. Apart from actin polymerisation, roles for other host processes in Listeria entry are unknown. Here, we demonstrate that exocytosis in the human cell promotes InlB-dependent internalisation. Using a probe consisting of VAMP3 with an exofacial green fluorescent protein tag, focal exocytosis was detected during InlB-mediated entry. Exocytosis was dependent on Met tyrosine kinase activity and the GTPase RalA. Depletion of SNARE proteins by small interfering RNA demonstrated an important role for exocytosis in Listeria internalisation. Depletion of SNARE proteins failed to affect actin filaments during internalisation, suggesting that actin polymerisation and exocytosis are separable host responses. SNARE proteins were required for delivery of the human GTPase Dynamin 2, which promotes InlB-mediated entry. Our results identify exocytosis as a novel host process exploited by Listeria for infection.

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“…F-BAR proteins possess a FCH-BAR (F-BAR) domain, which is a special BAR domain that binds lipids and induces membrane tubulation [23]. To further elucidate the physiological role of SNX9, we generated Snx9 knockout mice using homologous recombination method.…”

Section: Introductionmentioning

confidence: 99%

Sorting nexin 9 (SNX9) is not essential for development and auditory function in mice

Liu

Zhai

et al. 2016

Oncotarget

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Sorting nexins are a large family of evolutionarily conserved proteins that play fundamental roles in endocytosis, endosomal sorting and signaling. As an important member of sorting nexin family, sorting nexin 9 (SNX9) has been shown to participate in coordinating actin polymerization with membrane tubulation and vesicle formation. We previously showed that SNX9 is expressed in mouse auditory hair cells and might regulate actin polymerization in those cells. To further examine the physiological role of SNX9, we generated Snx9 knockout mice using homologous recombination method. Unexpectedly, Snx9 knockout mice have normal viability and fertility, and are morphologically and behaviorally indistinguishable from control mice. Further investigation revealed that the morphology and function of auditory hair cells are not affected by Snx9 inactivation, and Snx9 knockout mice have normal hearing threshold. In conclusion, our data revealed that Snx9-deficient mice do not show defects in development as well as auditory function, suggesting that SNX9 is not essential for mice development and hearing.

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Linking up at the BAR: Oligomerization and F-BAR protein function

Cited by 29 publications

References 109 publications

Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis

Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis

A role for host cell exocytosis in InlB-mediated internalisation ofListeria monocytogenes

Sorting nexin 9 (SNX9) is not essential for development and auditory function in mice

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