Regulation of Chaperone Effects on a Yeast Prion by Cochaperone Sgt2

Kiktev, Denis; Patterson, Jesse C.; Müller, Susanne; Bariar, Bhawana; Pan, Tao; Chernoff, Yury O.

doi:10.1128/mcb.00875-12

Cited by 58 publications

(77 citation statements)

References 70 publications

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“…Deletion of any of the five get genes impairs Hsp104 overproduction curing of [PSIϩ] without affecting Hsp104 levels or its other actions (186). An sgt2⌬ mutation interferes with the effects of get mutations or overproduction of Ssa1p in preventing [PSIϩ] curing by elevated Hsp104 (186). Sgt2p directly associates with Sup35p and Rnq1p in vivo (186) and with Get proteins and chaperones (157), suggesting that Sgt2p has a role in bringing these components together.…”

Section: Sgt2p the Get Pathway And [Psi؉]mentioning

confidence: 99%

“…Kiktev et al found that get2 mutation or deletion impairs curing of [PSIϩ] by overexpression of Hsp104 (186). The GET pathway (guided entry of tail-anchored proteins) prevents aggregation of proteins with hydrophobic tails destined for membrane sites and includes the Get1 and Get2 membrane components, cytoplasmic Get3, Get4, and Get5, and the cochaperone Sgt2p (157).…”

Section: Sgt2p the Get Pathway And [Psi؉]mentioning

confidence: 99%

“…An sgt2⌬ mutation interferes with the effects of get mutations or overproduction of Ssa1p in preventing [PSIϩ] curing by elevated Hsp104 (186). Sgt2p directly associates with Sup35p and Rnq1p in vivo (186) and with Get proteins and chaperones (157), suggesting that Sgt2p has a role in bringing these components together. Neither sgt2⌬ mutation nor overproduction of Sgt2p appears to affect [PSIϩ] propagation in an otherwise wild-type cell (186) …”

Section: Sgt2p the Get Pathway And [Psi؉]mentioning

confidence: 99%

“…The GET pathway (guided entry of tail-anchored proteins) prevents aggregation of proteins with hydrophobic tails destined for membrane sites and includes the Get1 and Get2 membrane components, cytoplasmic Get3, Get4, and Get5, and the cochaperone Sgt2p (157). Deletion of any of the five get genes impairs Hsp104 overproduction curing of [PSIϩ] without affecting Hsp104 levels or its other actions (186). An sgt2⌬ mutation interferes with the effects of get mutations or overproduction of Ssa1p in preventing [PSIϩ] curing by elevated Hsp104 (186).…”

Section: Sgt2p the Get Pathway And [Psi؉]mentioning

confidence: 99%

See 3 more Smart Citations

Yeast Prions: Structure, Biology, and Prion-Handling Systems

Wickner

Shewmaker

Bateman

et al. 2015

Microbiol Mol Biol Rev

131

142

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SUMMARY A prion is an infectious protein horizontally transmitting a disease or trait without a required nucleic acid. Yeast and fungal prions are nonchromosomal genes composed of protein, generally an altered form of a protein that catalyzes the same alteration of the protein. Yeast prions are thus transmitted both vertically (as genes composed of protein) and horizontally (as infectious proteins, or prions). Formation of amyloids (linear ordered β-sheet-rich protein aggregates with β-strands perpendicular to the long axis of the filament) underlies most yeast and fungal prions, and a single prion protein can have any of several distinct self-propagating amyloid forms with different biological properties (prion variants). Here we review the mechanism of faithful templating of protein conformation, the biological roles of these prions, and their interactions with cellular chaperones, the Btn2 and Cur1 aggregate-handling systems, and other cellular factors governing prion generation and propagation. Human amyloidoses include the PrP-based prion conditions and many other, more common amyloid-based diseases, several of which show prion-like features. Yeast prions increasingly are serving as models for the understanding and treatment of many mammalian amyloidoses. Patients with different clinical pictures of the same amyloidosis may be the equivalent of yeasts with different prion variants.

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Section: Sgt2p the Get Pathway And [Psi؉]mentioning

confidence: 99%

Section: Sgt2p the Get Pathway And [Psi؉]mentioning

confidence: 99%

Section: Sgt2p the Get Pathway And [Psi؉]mentioning

confidence: 99%

Section: Sgt2p the Get Pathway And [Psi؉]mentioning

confidence: 99%

See 2 more Smart Citations

Yeast Prions: Structure, Biology, and Prion-Handling Systems

Wickner

Shewmaker

Bateman

et al. 2015

Microbiol Mol Biol Rev

131

142

View full text Add to dashboard Cite

show abstract

“…Indeed, it is by inhibition of Hsp104 that guanidine cures prions (Ferreira et al 2001;Jung and Masison 2001;Jung et al 2002). Studies of other genes affecting the Hsp104-overproduction curing of [PSI+] have identified many other chaperones and nonchaperone components Newnam et al 1999;Allen et al 2007;Reidy and Masison 2010;Kiktev et al 2012). Curing of [URE3] by overproduced Ydj1p showed that Hsp40s could be involved in prion propagation (Moriyama et al 2000).…”

Section: Curing Yeast Prionsmentioning

confidence: 99%

Prions

Kryndushkin

Edskes

Shewmaker

et al. 2017

Cold Spring Harb Protoc

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Infectious proteins (prions) are usually self-templating filamentous protein polymers (amyloids). Yeast prions are genes composed of protein and, like the multiple alleles of DNA-based genes, can have an array of “variants,” each a distinct self-propagating amyloid conformation. Like the lethal mammalian prions and amyloid diseases, yeast prions may be lethal, or only mildly detrimental, and show an array of phenotypes depending on the protein involved and the prion variant. Yeast prions are models for both rare mammalian prion diseases and for several very common amyloidoses such as Alzheimer’s disease, type 2 diabetes, and Parkinson’s disease. Here, we describe their detection and characterization using genetic, cell biological, biochemical, and physical methods.

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Membrane Insertion of Tail‐anchored Proteins

Borgese

2015

Encyclopedia of Life Sciences

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Tail‐anchored proteins are a special class of transmembrane proteins, consisting of a cytosolic domain anchored to the phospholipid bilayer by a single hydrophobic segment adjacent to their most C‐terminus. Because of their particular topology, the C‐terminal anchor must be inserted into membranes post‐translationally by mechanisms that differ from the well‐known targeting/translocation co‐translational pathway. Recently, several advances have created a new understanding of the tail‐anchored protein insertion machinery. Because of the essential cellular roles carried out by tail‐anchored proteins, including vesicle fusion, regulation of apoptosis and formation of interorganellar contact sites, uncovering the machinery responsible for their biogenesis should further our ability to understand a wide variety of diseases such as forms of cancer caused by activation of the tail‐anchored protein oncogene BCL2. Key Concepts Tail‐anchored proteins have C‐terminal hydrophobic domains. Tail‐anchored proteins are inserted post‐translationally into the membrane. The GET complex inserts tail‐anchored proteins into the endoplasmic reticulum membrane in yeast. The TRC complex chaperones tail‐anchored proteins into endoplasmic reticulum membranes in mammals. The mitochondrial outer membrane appears to be the preferred destination of tail‐anchored proteins that fail to engage the GET/TRC complex. Functions of the GET/TRC pathway additional to tail‐anchored protein targeting are presently under intense investigation.

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Regulation of Chaperone Effects on a Yeast Prion by Cochaperone Sgt2

Cited by 58 publications

References 70 publications

Yeast Prions: Structure, Biology, and Prion-Handling Systems

Yeast Prions: Structure, Biology, and Prion-Handling Systems

Prions

Membrane Insertion of Tail‐anchored Proteins

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