TheSaccharomyces cerevisiae early secretion mutanttip20 is synthetic lethal with mutants in yeast coatomer and the SNARE proteins Sec22p and Ufe1p

Frigerio, Gabriella

doi:10.1002/(sici)1097-0061(199805)14:7<633::aid-yea267>3.0.co;2-3

Cited by 25 publications

(3 citation statements)

References 48 publications

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“…ufe1‐1 has the mutations S282N in the −2 layer and L295P (Lewis et al ., 1997). Synthetic lethality was described for a combination of ufe1‐1 and sec20‐1 (Frigerio, 1998), but not for sec20‐1 and sec22‐3 (Kaiser and Schekman, 1990). Mutations in SNAREs required for anterograde ER to Golgi traffic are not synthetically lethal with use1‐10AA even though they carry mutations in layer residues.…”

Section: Discussionmentioning

confidence: 99%

Use1p is a yeast SNARE protein required for retrograde traffic to the ER

et al. 2003

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SNAREs on transport vesicles and target membranes are required for vesicle targeting and fusion. Here we describe a novel yeast protein with a typical SNARE motif but with low overall amino acid homologies to other SNAREs. The protein localized to the endoplasmic reticulum (ER) and was therefore named Use1p (unconventional SNARE in the ER). A temperature‐sensitive use1 mutant was generated. use1 mutant cells accumulated the ER forms of carboxypeptidase Y and invertase. More specific assays revealed that use1 mutant cells were defective in retrograde traffic to the ER. This was supported by strong genetic interactions between USE1 and the genes encoding SNAREs in retrograde traffic to the ER. Antibodies directed against Use1p co‐immunoprecipitated the SNAREs Ufe1p, myc‐Sec20p and Sec22p, which form a SNARE complex required for retrograde traffic from the Golgi to the ER, but neither Bos1p nor Bet1p (members of the SNARE complex in anterograde traffic to the Golgi). Therefore, we conclude that Use1p is a novel SNARE protein that functions in retrograde traffic from the Golgi to the ER.

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Section: Discussionmentioning

confidence: 99%

Use1p is a yeast SNARE protein required for retrograde traffic to the ER

et al. 2003

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“…The Dsl1 complex is required for Ykt6 targeting to the PAS The Dsl1 complex (Dsl1, Dsl3, and Tip20) plays an important role in the retrograde vesicular transport from the Golgi to the ER. It supports the fusion between COPI-coated vesicles and the ER by binding the SNAREs Ufe1, Use1, and Sec20 (Frigerio, 1998;Kraynack et al, 2005;Ren et al, 2009;Meiringer et al, 2011). Moreover, the Dsl1 complex has also been connected to COPII-coated vesicles and their cargo, yet is an ER-resident complex (Andag et al, 2001;VanRheenen et al, 2001;Andag & Schmitt, 2003;Meiringer et al, 2011).…”

Section: Ykt6 Is Recruited To the Pas Prior To Autophagosome Completionmentioning

confidence: 97%

Function of the SNARE Ykt6 on autophagosomes requires the Dsl1 complex and the Atg1 kinase complex

et al. 2020

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The mechanism and regulation of fusion between autophagosomes and lysosomes/vacuoles are still only partially understood in both yeast and mammals. In yeast, this fusion step requires SNARE proteins, the homotypic vacuole fusion and protein sorting ( HOPS ) tethering complex, the RAB 7 GTP ase Ypt7, and its guanine nucleotide exchange factor ( GEF ) Mon1‐Ccz1. We and others recently identified Ykt6 as the autophagosomal SNARE protein. However, it has not been resolved when and how lipid‐anchored Ykt6 is recruited onto autophagosomes. Here, we show that Ykt6 is recruited at an early stage of the formation of these carriers through a mechanism that depends on endoplasmic reticulum ( ER )‐resident Dsl1 complex and COPII ‐coated vesicles. Importantly, Ykt6 activity on autophagosomes is regulated by the Atg1 kinase complex, which inhibits Ykt6 through direct phosphorylation. Thus, our findings indicate that the Ykt6 pool on autophagosomal membranes is kept inactive by Atg1 phosphorylation, and once an autophagosome is ready to fuse with vacuole, Ykt6 dephosphorylation allows its engagement in the fusion event.

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“…Mutation of Sec22 along with Tip20 appears to be lethal for S. cerevisiae because both of these proteins are required for vesicular transport between the ER and Golgi complex [40]. Tip20 is a cytoplasmic protein bound to the surface of the ER and is responsible for binding or un-coating of COP-I coated vesicles during retrograde transport.…”

Section: Role Of Sec22 In Yeastmentioning

confidence: 99%

Diverse Role of SNARE Protein Sec22 in Vesicle Trafficking, Membrane Fusion, and Autophagy

Adnan

Islam

Zhang

et al. 2019

Cells

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Protein synthesis begins at free ribosomes or ribosomes attached with the endoplasmic reticulum (ER). Newly synthesized proteins are transported to the plasma membrane for secretion through conventional or unconventional pathways. In conventional protein secretion, proteins are transported from the ER lumen to Golgi lumen and through various other compartments to be secreted at the plasma membrane, while unconventional protein secretion bypasses the Golgi apparatus. Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) proteins are involved in cargo vesicle trafficking and membrane fusion. The ER localized vesicle associated SNARE (v-SNARE) protein Sec22 plays a major role during anterograde and retrograde transport by promoting efficient membrane fusion and assisting in the assembly of higher order complexes by homodimer formation. Sec22 is not only confined to ER–Golgi intermediate compartments (ERGIC) but also facilitates formation of contact sites between ER and plasma membranes. Sec22 mutation is responsible for the development of atherosclerosis and symptoms in the brain in Alzheimer’s disease and aging in humans. In the fruit fly Drosophila melanogaster, Sec22 is essential for photoreceptor morphogenesis, the wingless signaling pathway, and normal ER, Golgi, and endosome morphology. In the plant Arabidopsis thaliana, it is involved in development, and in the nematode Caenorhabditis elegans, it is in involved in the RNA interference (RNAi) pathway. In filamentous fungi, it affects cell wall integrity, growth, reproduction, pathogenicity, regulation of reactive oxygen species (ROS), expression of extracellular enzymes, and transcriptional regulation of many development related genes. This review provides a detailed account of Sec22 function, summarizes its domain structure, discusses its genetic redundancy with Ykt6, discusses what is known about its localization to discrete membranes, its contributions in conventional and unconventional autophagy, and a variety of other roles across different cellular systems ranging from higher to lower eukaryotes, and highlights some of the surprises that have originated from research on Sec22.

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TheSaccharomyces cerevisiae early secretion mutanttip20 is synthetic lethal with mutants in yeast coatomer and the SNARE proteins Sec22p and Ufe1p

Cited by 25 publications

References 48 publications

Use1p is a yeast SNARE protein required for retrograde traffic to the ER

Use1p is a yeast SNARE protein required for retrograde traffic to the ER

Function of the SNARE Ykt6 on autophagosomes requires the Dsl1 complex and the Atg1 kinase complex

Diverse Role of SNARE Protein Sec22 in Vesicle Trafficking, Membrane Fusion, and Autophagy

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