ArticleMolecular biology of the cell2006
CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Transcriptome analysis of the brain provides insights into the regulatory mechanism for Coilia nasus migration.BMC genomics · 2020Article
- Upregulation of centromere protein F is linked to aggressive prostate cancers.Cancer management and research · 2018Article
- Loss of CENP-F results in distinct microtubule-related defects without chromosomal abnormalities.Molecular biology of the cell · 2016Article
- The kinetochore protein, CENPF, is mutated in human ciliopathy and microcephaly phenotypes.Journal of medical genetics · 2015Article
- Cardiac-specific deletion of the microtubule-binding protein CENP-F causes dilated cardiomyopathy.Disease models & mechanisms · 2012Article
- Hook2 is involved in the morphogenesis of the primary cilium.Molecular biology of the cell · 2011Article
- 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
- Proteomic analyses of retina of excitatory amino acid carrier 1 deficient mice.Proteome science · 2007Article
- Myosin V, Rab11, and dRip11 direct apical secretion and cellular morphogenesis in developing Drosophila photoreceptors.The Journal of cell biology · 2007Article
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Authors and funding
6 authors.
Funding
Abstract
SNAP-25 is a component of the SNARE complex that is involved in membrane docking and fusion. Using a yeast two-hybrid screen, we identify a novel interaction between SNAP-25 and cytoplasmic Lek1 (cytLEK1), a protein previously demonstrated to associate with the microtubule network. The binding domains within each protein were defined by yeast two-hybrid, coimmunoprecipitation, and colocalization studies. Confocal analyses reveal a high degree of colocalization between the proteins. In addition, the endogenous proteins can be isolated as a complex by immunoprecipitation. Further analyses demonstrate that cytLEK1 and SNAP-25 colocalize and coprecipitate with Rab11a, myosin Vb, VAMP2, and syntaxin 4, components of the plasma membrane recycling pathway. Overexpression of the SNAP-25-binding domain of cytLEK1, and depletion of endogenous Lek1 alters transferrin trafficking, consistent with a function in vesicle recycling. Taken together, our studies indicate that cytLEK1 is a link between recycling vesicles and the microtubule network through its association with SNAP-25. This interaction may play a key role in the regulation of the recycling endosome 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.