SLY1/YDR189W Summary Help

Standard Name SLY1
Systematic Name YDR189W
Feature Type ORF, Verified
Description Hydrophilic protein involved in ER/Golgi vesicle trafficking; SM (Sec1/Munc-18) family protein that binds the tSNARE Sed5p and stimulates its assembly into a trans-SNARE membrane-protein complex (1, 2 and see Summary Paragraph)
Name Description Suppressor of Loss of Ypt1
Chromosomal Location
ChrIV:838392 to 840392 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All SLY1 GO evidence and references
  View Computational GO annotations for SLY1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Resources
Classical genetics
conditional
null
repressible
Large-scale survey
conditional
null
overexpression
reduction of function
repressible
Resources
197 total interaction(s) for 128 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 15
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 25
  • Biochemical Activity: 1
  • Co-crystal Structure: 1
  • PCA: 7
  • Reconstituted Complex: 14
  • Two-hybrid: 6

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Lethality: 1
  • Dosage Rescue: 25
  • Negative Genetic: 60
  • Phenotypic Suppression: 8
  • Positive Genetic: 10
  • Synthetic Lethality: 14
  • Synthetic Rescue: 8

Resources
Expression Summary
histogram
Resources
Length (a.a.) 666
Molecular Weight (Da) 74,678
Isoelectric Point (pI) 4.94
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:838392 to 840392 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2001 838392..840392 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002597
SUMMARY PARAGRAPH for SLY1

Sly1p is an essential protein that is involved in protein trafficking between the ER and Golgi (3, 4, and reviewed in 5). Sly1p is involved in both anterograde transport from the ER to the Golgi as well as retrograde transport from the Golgi back to the ER (6, 7). Sly1p binding to the syntaxin SNARE Sed5p facilitates ER-derived transport vesicle fusion to the Golgi through the disassembly of cis-SNARE complexes/assembly of trans-SNARE complexes (2, 8, 9, 10). However, mutants that disrupt the high-affinity interaction between these two proteins indicate that the interaction between them may not be relevant for their proper function (11). Sly1p also interacts with SNAREs involved in retrograde Golgi to ER transport (Ufe1p, Use1p, Sec20p) and is involved in protecting the syntaxin SNARE Ufe1p against degradation (12, 13). Cells lacking Sly1p accumulate ER membranes and precursor forms of invertase and carboxypeptidase Y (4). Sly1p is a member of the Sec1/Munc-18 (SM) family of proteins and the other S. cerevisiae SM proteins include Sec1p, Vps33p, and Vps45p (reviewed in 5). Sly1p homologs have been identified in other organisms such as fission yeast, fly, rat, and human (14, 15, 16).

Last updated: 2010-05-12 Contact SGD

References cited on this page View Complete Literature Guide for SLY1
1) Cao X, et al.  (1998) Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J 17(8):2156-65
2) Kosodo Y, et al.  (2003) Cooperation of Sly1/SM-family protein and sec18/NSF of Saccharomyces cerevisiae in disassembly of cis-SNARE membrane-protein complexes. Biosci Biotechnol Biochem 67(2):448-50
3) Dascher C, et al.  (1991) Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily. Mol Cell Biol 11(2):872-85
4) Ossig R, et al.  (1991) The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Mol Cell Biol 11(6):2980-93
5) Halachmi N and Lev Z  (1996) The Sec1 family: a novel family of proteins involved in synaptic transmission and general secretion. J Neurochem 66(3):889-97
6) Lupashin VV, et al.  (1996) Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes. J Cell Biol 132(3):277-89
7) Li Y, et al.  (2005) Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum. Mol Biol Cell 16(9):3951-62
8) Lupashin VV and Waters MG  (1997) t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase. Science 276(5316):1255-8
9) Kosodo Y, et al.  (2002) Binding of Sly1 to Sed5 enhances formation of the yeast early Golgi SNARE complex. J Cell Sci 115(Pt 18):3683-91
10) Grabowski R and Gallwitz D  (1997) High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking. FEBS Lett 411(2-3):169-72
11) Peng R and Gallwitz D  (2004) Multiple SNARE interactions of an SM protein: Sed5p/Sly1p binding is dispensable for transport. EMBO J 23(20):3939-49
12) Yamaguchi T, et al.  (2002) Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev Cell 2(3):295-305
13) Braun S and Jentsch S  (2007) SM-protein-controlled ER-associated degradation discriminates between different SNAREs. EMBO Rep 8(12):1176-82
14) Li Y, et al.  (2007) Mutations of the SM protein Sly1 resulting in bypass of GTPase requirement in vesicular transport are confined to a short helical region. FEBS Lett 581(29):5698-702
15) Peterson MR, et al.  (1996) A mammalian homologue of SLY1, a yeast gene required for transport from endoplasmic reticulum to Golgi. Gene 169(2):293-4
16) Salzberg A, et al.  (1993) The Drosophila Ras2 and Rop gene pair: a dual homology with a yeast Ras-like gene and a suppressor of its loss-of-function phenotype. Development 117(4):1309-19