| + |
NEK6 | up-regulates activity 
phosphorylation
|
EML4 |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273883 |
Ser144 |
QSPQIRAsPSPQPSS |
in vitro |
|
| pmid |
sentence |
| 31409757 |
The mitotic kinases NEK6 and NEK7 phosphorylated the EML4 N-terminal domain at Ser144 and Ser146 in vitro, and depletion of these kinases in cells led to increased EML4 binding to microtubules in mitosis. An S144A-S146A double mutant not only bound inappropriately to mitotic microtubules but also increased their stability and interfered with chromosome congression. In addition, constitutive activation of NEK6 or NEK7 reduced the association of EML4 with interphase microtubules. Together, these data support a model in which NEK6- and NEK7-dependent phosphorylation promotes the dissociation of EML4 from microtubules in mitosis in a manner that is required for efficient chromosome congression. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NEK7 | up-regulates activity
phosphorylation
|
EML4 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273884 |
Ser146 |
PQIRASPsPQPSSQP |
in vitro |
|
| pmid |
sentence |
| 31409757 |
The mitotic kinases NEK6 and NEK7 phosphorylated the EML4 N-terminal domain at Ser144 and Ser146 in vitro, and depletion of these kinases in cells led to increased EML4 binding to microtubules in mitosis. An S144A-S146A double mutant not only bound inappropriately to mitotic microtubules but also increased their stability and interfered with chromosome congression. In addition, constitutive activation of NEK6 or NEK7 reduced the association of EML4 with interphase microtubules. Together, these data support a model in which NEK6- and NEK7-dependent phosphorylation promotes the dissociation of EML4 from microtubules in mitosis in a manner that is required for efficient chromosome congression. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
EML4
- 
- 