ArticleMolecular and cellular biochemistry2010
FEZ1 interacts with CLASP2 and NEK1 through coiled-coil regions and their cellular colocalization suggests centrosomal functions and regulation by PKC.
Article in Molecular and cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Loss of function of the ALS-associated NEK1 kinase disrupts microtubule homeostasis and nuclear import.Science advances · 2023Article
- Distinct Functions for Mammalian CLASP1 and -2 During Neurite and Axon Elongation.Frontiers in cellular neuroscience · 2019Article
- HIV-1 capsids bind and exploit the kinesin-1 adaptor FEZ1 for inward movement to the nucleus.Nature communications · 2015Article
- "Stop Ne(c)king around": How interactomics contributes to functionally characterize Nek family kinases.World journal of biological chemistry · 2014Review
- Nek1 interacts with Ku80 to assist chromatin loading of replication factors and S-phase progression.Cell cycle (Georgetown, Tex.) · 2013Article
- Crystal structure of the human short coiled coil protein and insights into SCOC-FEZ1 complex formation.PloS one · 2013Article
- FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.PloS one · 2011Article
- Human Nek6 is a monomeric mostly globular kinase with an unfolded short N-terminal domain.BMC structural biology · 2011Article
- NEK1 mutations cause short-rib polydactyly syndrome type majewski.American journal of human genetics · 2011Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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