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YKT6 Ykt6p

Ykt6, Ykt6p
This gene product is one of the SNARE recognition molecules implicated in vesicular transport between secretory compartments. It is a membrane associated, isoprenylated protein that functions at the endoplasmic reticulum-Golgi transport step. This protein is highly conserved from yeast to human and can functionally complement the loss of the yeast homolog in the yeast secretory pathway. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, BET1, CIs, Bos1p, v-SNARE
Papers on Ykt6
TANGO1 recruits ERGIC membranes to the endoplasmic reticulum for procollagen export.
Malhotra et al., Barcelona, Spain. In Elife, 2014
Along with the t-SNARE Syntaxin 18, we now reveal the complete complement of SNAREs required in this process, t-SNAREs BNIP1 and USE1, and v-SNARE YKT6.
Analysis of interactions between SNARE proteins using imaging ellipsometer coupled with microfluidic array.
Jiang et al., Beijing, China. In Sci Rep, 2013
In this study, we report the use of a label-free method, called imaging ellipsometer to analyze the interactions among three SNAREs, namely Sec22p, Ykt6p and Sso2p.
R-SNARE ykt6 resides in membrane-associated protease-resistant protein particles and modulates cell cycle progression when over-expressed.
Hay et al., Missoula, United States. In Biol Cell, 2012
BACKGROUND INFORMATION: The arginine-type soluble N-ethylmaleimide-sensitive factor attachment protein receptor (R-SNARE) ykt6 possesses several atypical properties including selective high expression in neurons, a lipidated C-terminus, localization to punctae that do not correspond with known endomembrane markers, a potent ability to protect the secretory pathway from alpha-synuclein over-expression and specific up-regulation in tumors.
Identification of Drosophila gene products required for phagocytosis of Leishmania donovani.
Smith et al., York, United Kingdom. In Plos One, 2011
Focussing on genes in the latter class, RNAi-mediated knockdown of the small GTPase Rab5, the prenylated SNARE protein YKT6, one sub-unit of serine palmitoyltransferase (spt2/lace), the Rac1-associated protein Sra1 and the actin cytoskeleton regulatory protein, SCAR, all lead to a significant reduction in parasite phagocytosis.
Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs.
Hay et al., Missoula, United States. In Mol Biol Cell, 2010
Ykt6 reversed alpha-synuclein inhibition much more effectively than sec22b, suggesting a possible neuroprotective role for the enigmatic high expression of ykt6 in neurons.
Lipid-Induced conformational switch controls fusion activity of longin domain SNARE Ykt6.
Zhang et al., Shanghai, China. In Mol Cell, 2010
A posttranslationally attached farnesyl group can actively regulate Ykt6 fusion activity in addition to its anticipated membrane-anchoring role.
Farnesylation of the SNARE protein Ykt6 increases its stability and helical folding.
Geyer et al., Dortmund, Germany. In J Mol Biol, 2008
Observations support a previously suggested closed conformation of cytosolic Ykt6, where the C-terminal farnesyl moiety folds onto a hydrophobic groove in the N-terminal longin domain.
Identification of gene transcripts in rat frontal cortex that are regulated by repeated electroconvulsive seizure treatment.
Chen et al., Taiwan. In Neuropsychobiology, 2007
The 4 upregulated genes are S100 protein, beta polypeptide (S100b), S100 calcium binding protein A13_predicted (S100a13_predicted), diazepam-binding inhibitor (Dbi), and YKT6 homolog (S.
Stimulation of actin polymerization by vacuoles via Cdc42p-dependent signaling.
Eitzen et al., Edmonton, Canada. In J Biol Chem, 2007
Affinity isolation of vacuole-associated actin and in vitro binding assays revealed a polymerization-dependent interaction between actin and the SNARE Ykt6p.
Possible involvement of CCT5, RGS3, and YKT6 genes up-regulated in p53-mutated tumors in resistance to docetaxel in human breast cancers.
Noguchi et al., Suita, Japan. In Breast Cancer Res Treat, 2007
mRNA expression of CCT5, RGS3, and YKT6 was significantly up-regulated in p53-mutated tumors and associated with a low response rate to docetaxel.
Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein.
Banfield et al., Hong Kong, Hong Kong. In Mol Biol Cell, 2006
Using nuclear magnetic resonance spectroscopy, we establish that the N-terminal domain of the yeast vacuolar R-SNARE Nyv1p adopts a longin-like fold similar to those of Sec22b and Ykt6p.
YKT6 is a core constituent of membrane fusion machineries at the Arabidopsis trans-Golgi network.
Bassham et al., Ames, United States. In J Mol Biol, 2005
In addition, we have identified two new functionally interchangeable components, YKT61 and YKT62, that show sequence similarity to the multifunctional yeast SNARE YKT6.
Identification of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer.
Jahn et al., Göttingen, Germany. In Mol Biol Cell, 2005
The sec22(Q)/sed5(R) mutant is temperature sensitive and is rescued by a compensating R-->Q replacement in the R-SNARE Ykt6p.
ATP-independent control of Vac8 palmitoylation by a SNARE subcomplex on yeast vacuoles.
Ungermann et al., Heidelberg, Germany. In J Biol Chem, 2005
during vacuole fusion, Nyv1 is the classical R-SNARE, whereas the Ykt6-containing complex has a novel function in Vac8 palmitoylation
The SNARE Ykt6 is released from yeast vacuoles during an early stage of fusion.
Ungermann et al., Heidelberg, Germany. In Embo Rep, 2005
Ykt6 is released from membranes by depalmitoylation
Molecular correlates of emotional learning using genetically selected rat lines.
Gershenfeld et al., Dallas, United States. In Genes Brain Behav, 2005
Four genes, Veli1 (mlin-7B), SLC3a1, Ptpro and Ykt6p, showed higher expression in SHA hippocampi than SLA.
An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p.
Zhang et al., Hong Kong, Hong Kong. In Science, 2001
Ykt6p is a nonsyntaxin SNARE implicated in multiple intracellular membrane trafficking steps.
Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs.
Schekman et al., Berkeley, United States. In Science, 1998
Other v-SNAREs, Sec22p and Ykt6p, might interact more weakly with the COPII coat or interact indirectly by binding to Bet1p or Bos1p.
A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles.
Söllner et al., New York City, United States. In Cell, 1994
We also report the identification of a novel v-SNARE (Ykt6p) component of the yeast ER-Golgi docking complex that has a CAAX box and is predicted to be lipid anchored.
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