Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/66898
Type: Artigo de periódico
Title: FEZ1 interacts with CLASP2 and NEK1 through coiled-coil regions and their cellular colocalization suggests centrosomal functions and regulation by PKC
Author: Lanza, DCF
Meirelles, GV
Alborghetti, MR
Abrile, CH
Lenz, G
Kobarg, J
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.
Subject: NIMA
CLIP
Cytoskeleton
Tubulin
Country: Holanda
Editor: Springer
Rights: fechado
Identifier DOI: 10.1007/s11010-009-0317-9
Date Issue: 2010
Appears in Collections:Unicamp - Artigos e Outros Documentos

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