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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

SAM and SH3 domain containing 3

SLY1, Sly, Sly1p
putative syntaxin-binding protein that regulates ER to Golgi transport [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: CAN, beta-glucuronidase, ACID, YPT1, V1a
Papers on SLY1
Large scale analysis of the mutational landscape in β-glucuronidase: A major player of mucopolysaccharidosis type VII.
New
Hassan et al., Durban, South Africa. In Gene, Feb 2016
Sly syndrome or mucopolysaccharidosis type VII is a lysosomal storage disorder associated with the deficiency of β-glucuronidase (EC 3.2.1.31)
Binding of GID1 to DELLAs promotes dissociation of GAF1 from DELLA in GA dependent manner.
New
Takahashi et al., Hiroshima, Japan. In Plant Signal Behav, Nov 2015
The sleepy1 (sly1) F-box mutant exhibits dwarfism and low-germination phenotypes due to high accumulation of DELLAs.
Functional characterization of an invertase inhibitor gene involved in sucrose metabolism in tomato fruit.
New
Wang et al., Shenyang, China. In J Zhejiang Univ Sci B, Oct 2015
In this study, we produced tomato plants overexpressing an invertase inhibitor gene (Sly-INH) from tomato, using a simple and efficient transient transformation system.
Toll-like receptor 4 confers inflammatory response to Suilysin.
Jiang et al., Beijing, China. In Front Microbiol, 2014
In this study, we found that suilysin (SLY) is the main protein inflammatory stimulus of SS2 and that native SLY (nSLY) stimulated cytokines independently of its haemolytic ability.
SASH1 inhibits proliferation and invasion of thyroid cancer cells through PI3K/Akt signaling pathway.
Zhang et al., Qingdao, China. In Int J Clin Exp Pathol, 2014
The SASH1 (SAM- and SH3-domain containing 1) gene, a member of the SLY-family of signal adapter proteins, has an important regulatory role in tumorigenesis, but its implication in thyroid carcinoma has not been yet investigated.
Transport according to GARP: receiving retrograde cargo at the trans-Golgi network.
Review
Hierro et al., Bethesda, United States. In Trends Cell Biol, 2011
X-ray crystallography of the Vps53 and Vps54 subunits of GARP has revealed that this complex is structurally related to other tethering factors such as the exocyst, the conserved oligomeric Golgi (COG) and Dsl1 (dependence on SLY1-20) complexes, indicating that they all might work by a similar mechanism.
The role of two f-box proteins, SLEEPY1 and SNEEZY, in Arabidopsis gibberellin signaling.
GeneRIF
Steber et al., Pullman, United States. In Plant Physiol, 2011
SNE function partly overlaps with SLY1 function in gibberellin signaling.
Dsl1p/Zw10: common mechanisms behind tethering vesicles and microtubules.
Review
Schmitt, Göttingen, Germany. In Trends Cell Biol, 2010
Fusion of Golgi-derived COP (coat protein)-I vesicles with the endoplasmic reticulum (ER) is initiated by specific tethering complexes: the Dsl1 (depends on SLY1-20) complex in yeast and the syntaxin 18 complex in mammalian cells.
Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing.
GeneRIF
Lev et al., Israel. In Embo J, 2009
Study shows that the SM protein, Sly1, interacts directly with the conserved oligomeric Golgi (COG) tethering complex; Sly1-COG interaction is mediated by the Cog4 subunit, which also interacts with Syntaxin 5 through a different binding site.
Mutations and polymorphisms in GUSB gene in mucopolysaccharidosis VII (Sly Syndrome).
Review
Sly et al., Saint Louis, United States. In Hum Mutat, 2009
Mucopolysaccharidosis VII (MPS VII; Sly syndrome) is an autosomal recessive disorder caused by a deficiency of beta-glucuronidase (GUS, EC 3.2.1.31;
Reduced notch activity is associated with an impaired marginal zone B cell development and function in Sly1 mutant mice.
GeneRIF
Beer et al., München, Germany. In Mol Immunol, 2009
expression of the Notch signaling mediator RBP-J and the Notch target genes Hes-1 and Hes-5 was markedly reduced in MZ but not FO B cells of Sly1(d/d) mice.
The orphan adapter protein SLY1 as a novel anti-apoptotic protein required for thymocyte development.
GeneRIF
Beer-Hammer et al., Düsseldorf, Germany. In Bmc Immunol, 2008
anti-apoptotic protein required for T cell differentiation to the CD4+CD8+ stage, likely to be involved in mTOR complex activation
Proteolysis-independent downregulation of DELLA repression in Arabidopsis by the gibberellin receptor GIBBERELLIN INSENSITIVE DWARF1.
GeneRIF
Steber et al., Pullman, United States. In Plant Cell, 2008
DELLA degradation causing GA responses requires GA biosynthesis, three functionally redundant GA receptors GIBBERELLIN INSENSITIVE DWARF1 (GID1a, b, and c), and the SLEEPY1 (SLY1) F-box subunit of an SCF E3 ubiquitin ligase.
Understanding gibberellic acid signaling--are we there yet?
Review
Schwechheimer, Tübingen, Germany. In Curr Opin Plant Biol, 2008
The current view is that GA binds to a soluble GID1 receptor, which interacts with the DELLA repressor proteins in a GA-dependent manner and thereby induces DELLA protein degradation via the E3 ubiquitin ligase SCF(GID2/SLY1).
Murine mucopolysaccharidosis VIL: impact of therapies on the phenotype, clinical course, and pathology in a model of a lysosomal storage disease.
Review
Sly et al., Saint Louis, United States. In Pediatr Dev Pathol, 2001
A murine model of MPS VII (Sly syndrome) has proven particularly useful because of its well-defined genetics and its well-characterized clinical, pathologic, and biochemical alterations, which resemble those seen in patients with mucopolysaccharidosis.
Low variability in a Y-linked plant gene and its implications for Y-chromosome evolution.
Impact
Charlesworth et al., Edinburgh, United Kingdom. In Nature, 2000
We have studied DNA diversity and divergence in a recently described X- and Y-linked gene pair (SLX-1 and SLY-1) of the plant Silene latifolia to obtain evidence about the early stages of Y degeneration.
Decreased lysosomal storage in the adult MPS VII mouse brain in the vicinity of grafts of retroviral vector-corrected fibroblasts secreting high levels of beta-glucuronidase.
Impact
Wolfe et al., Philadelphia, United States. In Nat Med, 1997
A deficiency of beta-glucuronidase (GUSB) causes the multisystem progressive degenerative syndrome, mucopolysaccharidosis (MPS) type VII (Sly disease), which includes mental retardation.
t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase.
Impact
Waters et al., Princeton, United States. In Science, 1997
Assembly of v-SNARE-t-SNARE targeting complexes is modulated by members of the Sec1-Sly1 protein family, and by small guanosine triphosphatases termed Rabs.
Neural progenitor cell engraftment corrects lysosomal storage throughout the MPS VII mouse brain.
Impact
Wolfe et al., Boston, United States. In Nature, 1995
We tested this approach in mucopolysaccharidosis VII (Sly disease), a lysosomal storage disorder of humans, dogs and mice caused by an inherited deficiency of beta-glucuronidase.
Reversal of pathology in murine mucopolysaccharidosis type VII by somatic cell gene transfer.
Impact
Birkenmeier et al., Bar Harbor, United States. In Nature, 1993
An inherited deficiency of beta-glucuronidase in humans, mice and dogs causes mucopolysaccharidosis VII (Sly syndrome), a progressive degenerative disease that reduces lifespan (to an average of 5 months in mice) and results from lysosomal storage of undegraded glycosaminoglycans in the spleen, liver, kidney, cornea, brain and skeletal system.
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