Endocytosis is essential for dynamic translocation of a syntaxin 1 orthologue during fission yeast meiosis

Kashiwazaki, Jun; Yamasaki, Yuriko; Itadani, Akiko; Teraguchi, Erika; Maeda, Yukari; Shimoda, Chikashi; Nakamura, Taro

doi:10.1091/mbc.e11-03-0255

Cited by 16 publications

(16 citation statements)

References 65 publications

(78 reference statements)

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“…The plasma membrane targeting syntaxin, Psy1, localizes all over the cell cortex during vegetative growth ( Maeda et al. , 2009 ; Kashiwazaki et al. , 2011 ), and the other t-SNARE Sec9 is not studied in detail.…”

Section: Discussionmentioning

confidence: 99%

Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis

Zhu

Hyun

Pan

et al. 2018

MBoC

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Cytokinesis is a complicated yet conserved step of the cell-division cycle that requires the coordination of multiple proteins and cellular processes. Here we describe a previously uncharacterized protein, Ync13, and its roles during fission yeast cytokinesis. Ync13 is a member of the UNC-13/Munc13 protein family, whose animal homologues are essential priming factors for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex assembly during exocytosis in various cell types, but no roles in cytokinesis have been reported. We find that Ync13 binds to lipids in vitro and dynamically localizes to the plasma membrane at cell tips during interphase and at the division site during cytokinesis. Deletion of Ync13 leads to defective septation and exocytosis, uneven distribution of cell-wall enzymes and components of cell-wall integrity pathway along the division site and massive cell lysis during cell separation. Interestingly, loss of Ync13 compromises endocytic site selection at the division plane. Collectively, we find that Ync13 has a novel function as an UNC-13/Munc13 protein in coordinating exocytosis, endocytosis, and cell-wall integrity during fission yeast cytokinesis.

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Section: Discussionmentioning

confidence: 99%

Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis

Zhu

Hyun

Pan

et al. 2018

MBoC

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“…2c), suggesting that Msy2 is localized in the cortical ER. To confirm this suggestion, we examined whether the signal of mCherry-Msy2 overlaps with that of reticulon-like protein (Rtn1)-EGFP, a cortical ER marker 24 and plasma-membrane proton-efflux P-type ATPase (Pma1)-EGFP, a plasma membrane marker 25 . The signals of mCherry-Msy2 generally merged with the signals of Rtn1-EGFP.…”

Section: Evolutionary Relationship Of Mscs Homologues In Fungimentioning

confidence: 99%

Organellar mechanosensitive channels in fission yeast regulate the hypo-osmotic shock response

2012

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A key molecule of sensing machineries essential for survival upon hypo-osmotic shock is the mechanosensitive channel. The bacterial mechanosensitive channel mscs functions directly for this purpose by releasing cytoplasmic solutes out of the cell, whereas plant mscs homologues are found to function in chloroplast organization. Here we show that the fission yeast mscs homologues, designated msy1 and msy2, participate in the hypo-osmotic shock response by a mechanism different from that operated by the bacterial mscs. upon hypoosmotic shock, msy2 -and msy1 -msy2 -cells display greater cell swelling than wild-type cells and undergo cell death. Cell swelling precedes an intracellular Ca 2 + increase, which was greater in msy1 -and msy1 -msy2 -cells than in wild-type cells. Fluorescent microscopy showed that msy1 and msy2 localize mainly to the endoplasmic reticulum. These observations suggest that organellar msy1 and msy2 regulate intracellular Ca 2 + and cell volume for survival upon hypo-osmotic shock.

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“…The distribution of F-actin during sporulation is well documented. F-actin dots seem to be randomly scattered in prophase I and become concentrated around the nucleus at the early stage of meiosis II (32,33). This behavior of F-actin is similar to that of Syb1, suggesting that, in sporulation, Syb1 localization is highly dependent on the actin cytoskeleton.…”

Section: Discussionmentioning

confidence: 92%

The Fission Yeast Synaptobrevin Ortholog Syb1 Plays an Important Role in Forespore Membrane Formation and Spore Maturation

et al. 2013

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Synaptobrevin, also called vesicle-associated membrane protein (VAMP), is a component of the plasma membrane N-methylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, which plays a key role in intracellular membrane fusion. Previous studies have revealed that, similar to synaptobrevin in other organisms, the fission yeast synaptobrevin ortholog Syb1 associates with post-Golgi secretory vesicles and is essential for cytokinesis and cell elongation. Here, we report that Syb1 has a role in sporulation. After nitrogen starvation, green fluorescent protein (GFP)-Syb1 is found in intracellular dots. As meiosis proceeds, GFP-Syb1 accumulates around the nucleus and then localizes at the forespore membrane (FSM). We isolated a syb-S1 mutant, which exhibits a defect in sporulation. In syb1-S1 mutants, the FSM begins to form but fails to develop a normal morphology. Electron microscopy shows that an abnormal spore wall is often formed in syb1-S1 mutant spores. Although most syb1-S1 mutant spores are germinated, they are less tolerant to ethanol than wild-type spores. The syb1-S1 allele carries a missense mutation, resulting in replacement of a conserved cysteine residue adjacent to the transmembrane domain, which reduces the stability and abundance of the Syb1 protein. Taken together, these results indicate that Syb1 plays an important role in both FSM assembly and spore wall formation. Members of the soluble N-methylmaleimide-sensitive factor attachment protein receptor (SNARE) family contribute to transport specificity by regulating interactions between membrane vesicles and their appropriate target membranes (1). SNARE proteins exist as complementary sets of v-SNAREs, found on vesicle membranes, and t-SNAREs, found on target membranes. Recent classification, however, takes into account the structural features of SNARE proteins, subdividing them into RSNAREs and Q-SNAREs (2).There are approximately 40 SNAREs in an animal cell, and each associates with a particular organelle in the biosyntheticsecretory or endocytic pathway (3). A v-SNARE is a single polypeptide chain, whereas a t-SNARE complex is composed of two or three proteins. The v-SNAREs and t-SNAREs have characteristic helical domains, and when a v-SNARE interacts with a t-SNARE, the helical domains of one wrap around the helical domains of the other to form a stable four-helix bundle. The resulting trans-SNARE complex locks the two membranes together.SNAREs have been well characterized in neurons, where they mediate the docking and fusion of synaptic vesicles at the nerve terminal's plasma membrane (PM) during the process of neurotransmitter release. The SNARE complex responsible for docking synaptic vesicles at the PM of nerve terminals consists of three proteins. The transmembrane proteins v-SNARE synaptobrevin (also called vesicle-associated membrane protein [VAMP]) and t-SNARE syntaxin each contribute one ␣-helix to the complex (4, 5), whereas the peripheral membrane protein t-SNARE SNAP-25 contributes two ␣-helices to the four-helix bun...

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Endocytosis is essential for dynamic translocation of a syntaxin 1 orthologue during fission yeast meiosis

Cited by 16 publications

References 65 publications

Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis

Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis

Organellar mechanosensitive channels in fission yeast regulate the hypo-osmotic shock response

The Fission Yeast Synaptobrevin Ortholog Syb1 Plays an Important Role in Forespore Membrane Formation and Spore Maturation

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