CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25.

Pooley RD, Reddy S, Soukoulis V, Roland JT, Goldenring JR, Bader DM
Mol Biol Cell. 2006 17 (7): 3176-86

PMID: 16672379 · PMCID: PMC1483049 · DOI:10.1091/mbc.e05-12-1127

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.

MeSH Terms (15)

Animals Cell Membrane Cells, Cultured Chromosomal Proteins, Non-Histone Endosomes Mice Microfilament Proteins Microtubules Protein Interaction Mapping Protein Structure, Tertiary Protein Transport Sequence Deletion Synaptosomal-Associated Protein 25 Transferrin Two-Hybrid System Techniques

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