The yeast dynamin-like protein Vps1:vps1 mutations perturb the internalization and the motility of endocytic vesicles and endosomes via disorganization of the actin cytoskeleton

Nannapaneni, Srikant; Wang, Daobing; Jain, Sandhya; Schroeder, Blake; Highfill, Chad; Reustle, Lindsay; Pittsley, Delilah; Maysent, Adam; Moulder, Shawn; McDowell, Ryan; Kim, Dong Kyu

doi:10.1016/j.ejcb.2010.02.002

Cited by 41 publications

(34 citation statements)

References 37 publications

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“…Here, we present data that we believe strongly support a role for the dynamin-like protein Vps1 in the endocytic process in Saccharomyces cerevisiae. Additional evidence for Vps1 function in endocytosis has also been recently reported by Nannapaneni and colleagues (Nannapaneni et al, 2010).…”

Section: Discussionmentioning

confidence: 69%

A role for the dynamin-like protein Vps1 during endocytosis in yeast

Rooij

Allwood

Aghamohammadzadeh

et al. 2010

Journal of Cell Science

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SummaryDynamins are a conserved family of proteins involved in membrane fusion and fission. Although mammalian dynamins are known to be involved in several membrane-trafficking events, the role of dynamin-1 in endocytosis is the best-characterised role of this protein family. Despite many similarities between endocytosis in yeast and mammalian cells, a comparable role for dynamins in yeast has not previously been demonstrated. The reported lack of involvement of dynamins in yeast endocytosis has raised questions over the general applicability of the current yeast model of endocytosis, and has also precluded studies using well-developed methods in yeast, to further our understanding of the mechanism of dynamin function during endocytosis. Here, we investigate the yeast dynamin-like protein Vps1 and demonstrate a transient burst of localisation to sites of endocytosis. Using live-cell imaging of endocytic reporters in strains lacking vps1, and also electron microscopy and biochemical approaches, we demonstrate a role for Vps1 in facilitating endocytic invagination. Vps1 mutants were generated, and analysis in several assays reveals a role for the C-terminal self-assembly domain in endocytosis but not in other membrane fission events with which Vps1 has previously been associated.

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Section: Discussionmentioning

confidence: 69%

A role for the dynamin-like protein Vps1 during endocytosis in yeast

Rooij

Allwood

Aghamohammadzadeh

et al. 2010

Journal of Cell Science

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“…2). Vps1 has previously been implicated in endocytosis (Nannapaneni et al, 2010;Smaczynska-de Rooij et al, 2012), similar to the known role of dynamin (Cocucci et al, 2012). At present, we do not yet know how Vps1 is recruited to the retromer tubules.…”

Section: Discussionmentioning

confidence: 91%

Retromer and the dynamin Vps1 cooperate in the retrieval of transmembrane proteins from vacuoles

Arlt

Reggiori

Ungermann

2014

Journal of Cell Science

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Endosomes are dynamic organelles that need to combine the ability to successfully deliver proteins and lipids to the lysosome-like vacuole, and recycle others to the Golgi or the plasma membrane. We now show that retromer, which is implicated in retrieval of proteins from endosomes to the Golgi or to the plasma membrane, can act on vacuoles. We explore its function using an assay that allows us to dissect the required cofactors during recycling. We demonstrate that recycling of the transmembrane receptor Vps10 from vacuoles requires the retromer, the dynamin-like Vps1, and the Rab7 GTPase Ypt7. Retromer and Vps1 leave the vacuole together with the cargo, whereas Ypt7 stays behind, in agreement with its regulatory function. Recycled cargo then accumulates at endosomes and later at the Golgi, implying consecutive sorting steps to the final destination. Our data further suggest that retromer and Vps1 are essential to maintain vacuole membrane organization. Taken together, our data demonstrate that retromer can cooperate with Vps1 and the Rab Ypt7 to clear the vacuole of selected membrane proteins.

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“…The lifetime an Abp1-RFP patch at the membrane (from the time of its appearance to the time at which it moves away from its origin or disappears) was determined as described previously (Nannapaneni et al 2010). A total of 20-25 patches were measured to determine the average patch lifespan of a strain.…”

Section: Actin Staining With Fluorescein Isothiocyanatephalloidinmentioning

confidence: 99%

“…Yeast strains expressing Pil1-RFP, Pma1-RFP, Abp1-RFP or Slm1-GFP were constructed by integrating the respective RFP or GFP constructs at the 3′ end of the PIL1-, PMA1-, ABP1-or SLM1-coding regions as described previously (Longtine et al 1998;Kim et al 2006;Nannapaneni et al 2010) in a wild-type haploid (BY 4741 or 4742). Similarly, Slm1-GFP in pil1Δ, Pil1-GFP in slm1Δ, Pil1-RFP in slm1Δ, and Pil1-RFP or Abp1-RFP in slm1-2slm2Δ and slm1-3slm2Δ were constructed by integrating the respective RFP or GFP constructs in each mutant strain.…”

Section: Yeast Strain Construction and Mediamentioning

confidence: 99%

Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae

et al. 2011

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Eisosomes are large immobile assemblies at the cortex of a cell under the membrane compartment of Can1 (MCC) in yeast. Slm1 has recently been identified as an MCC component that acts downstream of Mss4 in a pathway that regulates actin cytoskeleton organization in response to stress. In this study, we showed that inactivation of Slm proteins disrupts proper localization of the primary eisosome marker Pil1, providing evidence that Slm proteins play a role in eisosome organization. Furthermore, we found that slm ts mutant cells exhibit actin defects in both the ability to polarize cortical F-actin and the formation of cytoplasmic actin cables even at the permissive temperature (30 degrees C). We further demonstrated that the actin defect accounts for the slow traffic of FM4-64- labelled endosome in the cytoplasm, supporting the notion that intact actin is essential for endosome trafficking. However, our real-time microscopic analysis of Abp1-RFP revealed that the actin defect in slm ts cells was not accompanied by a noticeable defect in actin patch internalization during receptor-mediated endocytosis. In addition, we found that slm ts cells displayed impaired membrane recycling and that recycling occurred in an actin-independent manner. Our data provide evidence for the requirement of Slm proteins in eisosome organization and endosome trafficking and recycling.

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The yeast dynamin-like protein Vps1:vps1 mutations perturb the internalization and the motility of endocytic vesicles and endosomes via disorganization of the actin cytoskeleton

Cited by 41 publications

References 37 publications

A role for the dynamin-like protein Vps1 during endocytosis in yeast

A role for the dynamin-like protein Vps1 during endocytosis in yeast

Retromer and the dynamin Vps1 cooperate in the retrieval of transmembrane proteins from vacuoles

Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae

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