11 research outputs found
Consequences of soil compaction for seedling establishment: Implications for natural regeneration and restoration
The effect of constant darkness on the content of adipokinetic hormone, adipokinetic response and walking activity in macropterous females of Pyrrhocoris apterus (L.)
Minerals and Heavy Metals in the Whole Raw Milk of Dairy Cows from Different Management Systems and Countries of Origin: A Meta-Analytical Study
Lipid mobilization and locomotor stimulation in Gryllus bimaculatus by topically applied adipokinetic hormone
Hormonal modulation of glycogen reserves In the fat body of castor semilooperAchaea janata Linn (Lepidoptera, Noctuidea)
Disulfide connectivity and reduction in pheromone-binding proteins of the gypsy moth, Lymantria dispar
CytLEK1 Is a Regulator of Plasma Membrane Recycling through Its Interaction with SNAP-25
SNAP-25 is a component of the SNARE complex that is involved in membrane docking and fusion. Using a yeast two-hybrid screen, we identify a novel interaction between SNAP-25 and cytoplasmic Lek1 (cytLEK1), a protein previously demonstrated to associate with the microtubule network. The binding domains within each protein were defined by yeast two-hybrid, coimmunoprecipitation, and colocalization studies. Confocal analyses reveal a high degree of colocalization between the proteins. In addition, the endogenous proteins can be isolated as a complex by immunoprecipitation. Further analyses demonstrate that cytLEK1 and SNAP-25 colocalize and coprecipitate with Rab11a, myosin Vb, VAMP2, and syntaxin 4, components of the plasma membrane recycling pathway. Overexpression of the SNAP-25–binding domain of cytLEK1, and depletion of endogenous Lek1 alters transferrin trafficking, consistent with a function in vesicle recycling. Taken together, our studies indicate that cytLEK1 is a link between recycling vesicles and the microtubule network through its association with SNAP-25. This interaction may play a key role in the regulation of the recycling endosome pathway