Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport.

Pooley RD, Moynihan KL, Soukoulis V, Reddy S, Francis R, Lo C, Ma LJ, Bader DM
J Cell Sci. 2008 121 (Pt 20): 3413-21

PMID: 18827011 · PMCID: PMC2849733 · DOI:10.1242/jcs.032847

Syntaxin 4 is a component of the SNARE complex that regulates membrane docking and fusion. Using a yeast two-hybrid screen, we identify a novel interaction between syntaxin 4 and cytoplasmic murine CENPF, a protein previously demonstrated to associate with the microtubule network and SNAP-25. The binding domain for syntaxin 4 in CENPF was defined by yeast two-hybrid assay and co-immunoprecipitation. Confocal analyses in cell culture reveal a high degree of colocalization between endogenously expressed proteins in interphase cells. Additionally, the endogenous SNARE proteins can be isolated as a complex with CENPF in immunoprecipitation experiments. Further analyses demonstrate that murine CENPF and syntaxin 4 colocalize with components of plasma membrane recycling: SNAP-25 and VAMP2. Depletion of endogenous CENPF disrupts GLUT4 trafficking whereas expression of a dominant-negative form of CENPF inhibits cell coupling. Taken together, these studies demonstrate that CENPF provides a direct link between proteins of the SNARE system and the microtubule network and indicate a diverse role for murine CENPF in vesicular transport.

MeSH Terms (18)

Animals Biological Transport Cell Membrane Cercopithecus aethiops Chromosomal Proteins, Non-Histone COS Cells Cytoplasm Glucose Transporter Type 4 Mice Microfilament Proteins Microtubules NIH 3T3 Cells Qa-SNARE Proteins Saccharomyces cerevisiae Synaptosomal-Associated Protein 25 Transport Vesicles Two-Hybrid System Techniques Vesicle-Associated Membrane Protein 2

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