Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person At mitotic entry, EML4 undergoes phosphorylation on serine a...
| Class:Id | Summation:9648104 |
|---|---|
| _displayName | At mitotic entry, EML4 undergoes phosphorylation on serine a... |
| _timestamp | 2019-10-02 18:47:05 |
| created | [InstanceEdit:9648098] Orlic-Milacic, Marija, 2019-06-04 |
| modified | [InstanceEdit:9663523] Orlic-Milacic, Marija, 2019-10-02 |
| text | At mitotic entry, EML4 undergoes phosphorylation on serine and/or threonine residues (Pollmann et al. 2006). NEK6 and NEK7 serine/threonine kinases phosphorylate EML4 at evolutionarily conserved serine residues S144 and S146. Phosphorylation of EML4 at S144 and S146 reduces the affinity of EML4 for microtubules, leading to an increase in microtubule instability that is necessary for the assembly of a dynamic mitotic spindle and successful segregation of duplicated chromosomes (Adib et al. 2019). |
| (summation) | [Reaction:9648089] NEK6 and NEK7 phosphorylate EML4 [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by At mitotic entry, EML4 undergoes phosphorylation on serine a... (9648104)
