ArticleProceedings of the National Academy of Sciences of the United States of America2005
Cytoplasmic LEK1 is a regulator of microtubule function through its interaction with the LIS1 pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- 3β, 6β-dichloro-5-hydroxy-5α-cholestane facilitates neuronal development through modulating TrkA signaling regulated proteins in primary hippocampal neuron.Scientific reports · 2019Article
- Nde1 promotes diverse dynein functions through differential interactions and exhibits an isoform-specific proteasome association.Molecular biology of the cell · 2018Article
- Disentangling the molecular determinants for Cenp-F localization to nuclear pores and kinetochores.EMBO reports · 2018Article
- Regulation of Cenp-F localization to nuclear pores and kinetochores.Cell cycle (Georgetown, Tex.) · 2018Article
- Loss of CENP-F results in distinct microtubule-related defects without chromosomal abnormalities.Molecular biology of the cell · 2016Article
- Identification of Rare, Single-Nucleotide Mutations in NDE1 and Their Contributions to Schizophrenia Susceptibility.Schizophrenia bulletin · 2015Article
- The kinetochore protein, CENPF, is mutated in human ciliopathy and microcephaly phenotypes.Journal of medical genetics · 2015Article
- NDE1 and NDEL1: twin neurodevelopmental proteins with similar 'nature' but different 'nurture'.Biomolecular concepts · 2013Review
- Cardiac-specific deletion of the microtubule-binding protein CENP-F causes dilated cardiomyopathy.Disease models & mechanisms · 2012Article
- Rab11-FIP2 influences multiple components of the endosomal system in polarized MDCK cells.Cellular logistics · 2011Article
- Regulators of the cytoplasmic dynein motor.Nature reviews. Molecular cell biology · 2009Review
- Murine CENP-F regulates centrosomal microtubule nucleation and interacts with Hook2 at the centrosome.Molecular biology of the cell · 2009Article
- Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport.Journal of cell science · 2008Article
- Involvement of LEK1 in dendritic cell regulation of T cell immunity against Chlamydia.Journal of immunology (Baltimore, Md. : 1950) · 2008Article
- Elucidating the relationship between DISC1, NDEL1 and NDE1 and the risk for schizophrenia: evidence of epistasis and competitive binding.Human molecular genetics · 2008Article
- Bves directly interacts with GEFT, and controls cell shape and movement through regulation of Rac1/Cdc42 activity.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- NudE and NudEL are required for mitotic progression and are involved in dynein recruitment to kinetochores.The Journal of cell biology · 2007Article
- CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25.Molecular biology of the cell · 2006Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
LIS1 and nuclear distribution gene E (NudE) are partner proteins in a conserved pathway regulating the function of dynein and microtubules. Here, we present data that cytoplasmic LEK1 (cytLEK1), a large protein containing a spectrin repeat and multiple leucine zippers, is a component of this pathway through its direct interaction with NudE, as determined by a yeast two-hybrid screen. We identified the binding domains in each molecule, and coimmunoprecipitation and colocalization studies confirmed the specificity of the interaction between cytLEK1 and NudE. Confocal deconvolution analysis revealed that cytLEK1 exhibits colocalization with endogenous NudE and with the known NudE binding partners, LIS1 and dynein. By localizing the NudE-binding domain of cytLEK1 to a small domain within the molecule, we were able to disrupt cytLEK1 function by using a dominant negative approach in addition to LEK1 knockdown and, thus, examine the role of the cytLEK1-NudE interaction in cells. Consistent with a defect in the LIS1 pathway, disruption of cytLEK1 function resulted in alteration of microtubule organization and cellular shape. The microtubule network of cells became tightly focused around the nucleus and resulted in a rounded cell shape. Additionally, cells exhibited a severe inability to repolymerize their microtubule networks after nocodazole challenge. Taken together, our studies revealed that cytLEK1 is essential for cellular functions regulated by the LIS1 pathway.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.