High impact information on EML4

• Most importantly, EML4 negative cells showed a completely modified microtubule network, indicating that EML4 is necessary for correct microtubule formation [1].
• In no case mitotic figures could be observed in EML4 negative HeLa cells [1].
• Immunoprecipitation experiments revealed that EML4 is hyperphosphorylated on serine/threonine residues during mitosis [1].
• In addition, immunofluorescence stainings demonstrated that hyperphosphorylated EML4 is associated with the mitotic spindle, suggesting that the function of EML4 is regulated by phosphorylation. siRNA-mediated knockdown of EML4 in HeLa cells led to a significant decrease in the number of cells [1].
• Correspondingly, immunofluorescence stainings and transient expression of EGFP-labeled EML4 revealed a complete colocalization of EML4 with the interphase microtubule array of HeLa cells [1].

Biological context of EML4

• The gene encoding ropp120 (HGMW-approved gene symbol C2orf2) was assigned to chromosome 2p21-p22 by means of radiation hybrid and fluorescence in situ hybridization mapping [2].
• Indeed, transient transfection of GFP-Eml4 resulted in a marked decrease in the microtubule growth rate, which is in line with our hypothesis that Eml4 functions as a microtubule stabilizing protein [3].

Anatomical context of EML4

• We present evidence that the amino-terminal portion of EML4 (amino acids 1-249) is essential for the association with microtubules [1].
• Spatially, Eml4 expression becomes restricted to the olfactory bulb, hippocampus and cerebellum [3].

Associations of EML4 with chemical compounds

• In addition, transient overexpression of GFP-Eml4 in Cos7 cells resulted in microtubules that were resistant to nocodazole treatment suggesting that Eml4 stabilizes microtubules [3].

References