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Updated: Jun 18, 2026

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
Published on: August 13, 2012
FEZ1 interacts with CLASP2 and NEK1 through coiled-coil regions and their cellular colocalization suggests
Daniel C F Lanza1, Gabriela V Meirelles, Marcos R Alborghetti
1Centro de Biologia Molecular Estrutural, Associação Brasileira de Tecnologia de Luz Síncrotron, Rua Giuseppe Máximo Scolfaro, Campinas, SP, Brazil.
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.
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