Ykt6p, a Prenylated SNARE Essential for Endoplasmic Reticulum-Golgi Transport

McNew, James A.; Søgaard, Morten; Lampen, Nina; Machida, Sachiko; Ye, R. Ruby; Lacomis, Lynne; Tempst, Paul; Rothman, James E.; Söllner, Thomas H.

doi:10.1074/jbc.272.28.17776

Cited by 224 publications

(232 citation statements)

References 59 publications

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“…For example, Vti1p is involved in Golgi to vacuole trafficking (62,63), whereas Ykt6p is a v-SNARE that plays a role in trafficking through the Golgi (64,65). Both of these proteins also play a role in homotypic vacuolar fusion (51).…”

Section: Fig 5 Ypt7p Is Necessary For the Degradation Of Fbpase Andmentioning

confidence: 99%

The Vid Vesicle to Vacuole Trafficking Event Requires Components of the SNARE Membrane Fusion Machinery

Brown

Liu

Hung

et al. 2003

Journal of Biological Chemistry

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Lysosomal protein degradation is induced when cultured cells are starved of nutrients or serum. This process recycles amino acids and allows for the synthesis of proteins that are crucial for cell survival during starvation. Several mechanisms are responsible for increased lysosomal degradation during starvation (1-5). The macroautophagy pathway utilizes autophagosomes to deliver cytosolic proteins and organelles to lysosomes for degradation. The chaperone-mediated autophagy pathway targets cytosolic proteins containing a KFERQ motif for degradation. These proteins are recognized by the heat shock protein hsc73 and a lysosomal receptor LGP96 (1, 6 -9).

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Section: Fig 5 Ypt7p Is Necessary For the Degradation Of Fbpase Andmentioning

confidence: 99%

The Vid Vesicle to Vacuole Trafficking Event Requires Components of the SNARE Membrane Fusion Machinery

Brown

Liu

Hung

et al. 2003

Journal of Biological Chemistry

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“…Several v-SNAREs with functions in traffic from the ER to the Golgi apparatus or in retrograde traffic within the Golgi apparatus have been identified in yeast: Sec22p/Sly2p, Bet1p/Sly12p, Bos1p, Sft1p, Ykt6p, and Gos1p (Newman et al, 1990;Ossig et al, 1991;McNew et al, 1997;Holthuis et al, 1998a). The v-SNAREs Snc1p and Snc2p interact with Sso1p and Sso2p in secretion (Protopopov et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

TheSaccharomyces cerevisiaev-SNARE Vti1p Is Required for Multiple Membrane Transport Pathways to the Vacuole

Mollard

Stevens

1999

MBoC

162

133

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The interaction between v-SNAREs on transport vesicles and t-SNAREs on target membranes is required for membrane traffic in eukaryotic cells. Here we identify Vti1p as the first v-SNARE protein found to be required for biosynthetic traffic into the yeast vacuole, the equivalent of the mammalian lysosome. Certain vti1-tsyeast mutants are defective in alkaline phosphatase transport from the Golgi to the vacuole and in targeting of aminopeptidase I from the cytosol to the vacuole. VTI1 interacts genetically with the vacuolar t-SNARE VAM3, which is required for transport of both alkaline phosphatase and aminopeptidase I to the vacuole. The v-SNARE Nyv1p forms a SNARE complex with Vam3p in homotypic vacuolar fusion; however, we find that Nyv1p is not required for any of the three biosynthetic pathways to the vacuole. v-SNAREs were thought to ensure specificity in membrane traffic. However, Vti1p also functions in two additional membrane traffic pathways: Vti1p interacts with the t-SNAREs Pep12p in traffic from the TGN to the prevacuolar compartment and with Sed5p in retrograde traffic to the cis-Golgi. The ability of Vti1p to mediate multiple fusion steps requires additional proteins to ensure specificity in membrane traffic.

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“…Unexpectedly, the structure of SEDL is closely similar to those of the N-terminal domain of SNAREs Ykt6p and mouse Sec22b (mSec22b). The yeast SNARE Ykt6p has been implicated in several trafficking steps, including vesicle transport from the ER-to-Golgi and intra-Golgi transport (20). Its mammalian homologue was shown to function in the late step of ER-to-Golgi transport (21).…”

mentioning

confidence: 99%

Crystal Structure of SEDL and Its Implications for a Genetic Disease Spondyloepiphyseal Dysplasia Tarda

Jang

Kim

Cho

et al. 2002

Journal of Biological Chemistry

100

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SEDL is an evolutionarily highly conserved protein in eukaryotic organisms. Deletions or point mutations in the SEDL gene are responsible for the genetic disease spondyloepiphyseal dysplasia tarda (SEDT), an X-linked skeletal disorder. SEDL has been identified as a component of the transport protein particle (TRAPP), critically involved in endoplasmic reticulum-to-Golgi vesicle transport. Herein, we report the 2.4 Å resolution structure of SEDL, which reveals an unexpected similarity to the structures of the N-terminal regulatory domain of two SNAREs, Ykt6p and Sec22b, despite no sequence homology to these proteins. The similarity and the presence of unusually many solvent-exposed apolar residues of SEDL suggest that it serves regulatory and/or adaptor functions through multiple protein-protein interactions. Of the four known missense mutations responsible for SEDT, three mutations (S73L, F83S, V130D) map to the protein interior, where the mutations would disrupt the structure, and the fourth (D47Y) on a surface at which the mutation may abrogate functional interactions with a partner protein.Intracellular targeting and fusion of transport vesicles in eukaryotes are tightly regulated to avoid inappropriate mixing of the contents in different compartments. Central components of the membrane fusion are the proteins denoted as SNAREs 1 (soluble N-ethylmaleimide-sensitive factor attachment receptor proteins). SNAREs constitute a superfamily of proteins that share a highly conserved sequence motif, the SNARE motif composed of 60 -70 amino acids (1). Most SNAREs are membrane proteins anchored on vesicular carriers (v-SNARE) and target organelles (t-SNARE) (1). Association of the SNARE domains between v-and t-SNAREs to form a helical bundle, termed the core complex (2), is believed to be the prime event that drives membrane fusion (3, 4). While the specific pairing of v-and t-SNAREs is one mechanism of providing the fidelity of membrane fusion, other proteins or protein complexes such as the transport protein particle (TRAPP) are known to provide further specificity by controlling the tethering process, in which a transport vesicle is properly docked on target membrane prior to pairing of SNAREs (5). TRAPP is localized to an early Golgi compartment (6) and is able to exchange the nucleotide of Ypt1p GTPase, which is an upstream event of v-and t-SNARE interactions (7,8). Recent in vitro transport studies showed that yeast TRAPP I binds COPII, the vesicle coat derived from the endoplasmic reticulum (ER), indicating that TRAPP I is the receptor for tethering COPII vesicles to Golgi membranes (6). The TRAPP complexes (TRAPP I and TRAPP II) are composed of 7-10 different polypeptides, which are highly conserved in evolution, with the yeast subunits sharing between 29 and 54% sequence identity with their human counterparts (9). The biochemical function of any of the constituent proteins is virtually unknown, although the TRAPP complex was shown to stimulate nucleotide exchange on the Ypt1p and the Ypt31/32 GTPases (10).Spond...

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Ykt6p, a Prenylated SNARE Essential for Endoplasmic Reticulum-Golgi Transport

Cited by 224 publications

References 59 publications

The Vid Vesicle to Vacuole Trafficking Event Requires Components of the SNARE Membrane Fusion Machinery

The Vid Vesicle to Vacuole Trafficking Event Requires Components of the SNARE Membrane Fusion Machinery

TheSaccharomyces cerevisiaev-SNARE Vti1p Is Required for Multiple Membrane Transport Pathways to the Vacuole

Crystal Structure of SEDL and Its Implications for a Genetic Disease Spondyloepiphyseal Dysplasia Tarda

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