Abstract
FEZ1 was initially described as a neuronal protein that influences axonal development and cell polarization. CLASP2 and NEK1 proteins are present in a centrosomal complex and participate in cell cycle and cell division mechanisms, but their functions were always described individually. Here, we report that NEK1 and CLASP2 colocalize with FEZ1 in a perinuclear region in mammalian cells, and observed that coiled-coil interactions occur between FEZ1/CLASP2 and FEZ1/NEK1 in vitro. These three proteins colocalize and interact with endogenous gamma-tubulin. Furthermore, we found that CLASP2 is phosphorylated and interacts with active PKC isoforms, and that FEZ1/CLASP2 colocalization is inhibited by PMA treatment. Our results provide evidence that these three proteins cooperate in centrosomal functions and open new directions for future studies.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing / genetics
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Adaptor Proteins, Signal Transducing / metabolism*
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Animals
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Cell Cycle Proteins / genetics
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Cell Cycle Proteins / metabolism*
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Cell Line
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Cell Nucleus / metabolism
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Centrosome / metabolism*
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Humans
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Isoenzymes / genetics
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Isoenzymes / metabolism
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Microtubule-Associated Proteins / genetics
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Microtubule-Associated Proteins / metabolism*
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NIMA-Related Kinase 1
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism*
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Protein Binding
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Protein Kinase C / genetics
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Protein Kinase C / metabolism*
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism*
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Protein Structure, Tertiary*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Tubulin / metabolism
Substances
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Adaptor Proteins, Signal Transducing
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CLASP2 protein, human
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Cell Cycle Proteins
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FEZ1 protein, human
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Isoenzymes
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Microtubule-Associated Proteins
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Nerve Tissue Proteins
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Recombinant Fusion Proteins
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Tubulin
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NEK1 protein, human
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NIMA-Related Kinase 1
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Protein Serine-Threonine Kinases
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Protein Kinase C