High impact information on YKT6

• Here we present the structure of the NH2-terminal domain of Ykt6p (Ykt6pN, residues 1 to 140) [1].
• Ykt6p is a nonsyntaxin SNARE implicated in multiple intracellular membrane trafficking steps [1].
• The NH2-terminal domain plays an important biological role in the function of Ykt6p, which in vitro studies revealed to include influencing the kinetics and proper assembly of SNARE complexes [1].
• In mammals, TI-VAMP and Ykt6 are crucial for neuronal function, and defects in longin structure or function might underlie some human neurological pathologies [2].
• The functions and cellular localization of longins are regulated at several levels and the longin prototypes TI-VAMP, Sec22 and Ykt6 show different distributions among eukaryotes, reflecting their modular and functional diversity [2].

Biological context of YKT6

• The N-terminal domain of human Ykt6 contains a Pal-CoA binding site and is required for the reaction [3].
• Treatment of MCF-7 cells with siRNA specific for CCT5, RGS3, or YKT6 resulted in a significant enhancement of docetaxel-induced apoptosis [4].
• Farnesylation is the prerequisite for subsequent palmitoylation of the upstream cysteine, which permits stable membrane association of Ykt6 [5].
• YKT6 is an essential gene that codes for a novel vesicle-associated SNARE functioning at the endoplasmic reticulum-Golgi transport step in the yeast secretory pathway [6].
• Herein, we report the 2.4 A 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 [7].

Anatomical context of YKT6

• Ykt6 is highly enriched in the cerebral cortex and hippocampus and is targeted to a novel compartment in neurons [8].
• Depletion of Ykt6p results in the accumulation of the p1 precursor (endoplasmic reticulum form) of the vacuolar enzyme carboxypeptidase Y and morphological abnormalities consistent with a defect in secretion [6].
• The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion [9].
• The conservation of Ykt6 and its localization to several organelles suggest that its acyltransferase activity may also be required in other intracellular fusion events [9].

Associations of YKT6 with chemical compounds

• The human SNARE protein Ykt6 mediates its own palmitoylation at C-terminal cysteine residues [3].

References