| + |
CEP135 | up-regulates activity 
binding
|
SASS6 |
0.616 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269676 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23511974 |
In this study, we demonstrate that the human microcephaly protein, CEP135, directly interacts with hSAS-6 via its carboxyl-terminus and with MTs via its amino-terminus. Unexpectedly, CEP135 also interacts with another microcephaly protein CPAP via its amino terminal domain. Depletion of CEP135 not only perturbed the centriolar localization of CPAP, but also blocked CPAP-induced centriole elongation. We propose that CEP135 may serve as a linker protein that directly connects the central hub protein, hSAS-6, to the outer MTs, and suggest that this interaction stabilizes the proper cartwheel structure for further CPAP-mediated centriole elongation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CEP135 | up-regulates activity
binding
|
CENPJ |
0.802 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269677 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23511974 |
In this study, we demonstrate that the human microcephaly protein, CEP135, directly interacts with hSAS-6 via its carboxyl-terminus and with MTs via its amino-terminus. Unexpectedly, CEP135 also interacts with another microcephaly protein CPAP via its amino terminal domain. Depletion of CEP135 not only perturbed the centriolar localization of CPAP, but also blocked CPAP-induced centriole elongation. We propose that CEP135 may serve as a linker protein that directly connects the central hub protein, hSAS-6, to the outer MTs, and suggest that this interaction stabilizes the proper cartwheel structure for further CPAP-mediated centriole elongation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CEP135 | up-regulates activity
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269678 |
|
|
in vitro |
|
| pmid |
sentence |
| 27477386 |
Here, we analyzed in detail the microtubule-binding activity of human CEP135 (HsCEP135). Biochemical, cryo-electron, and fluorescence microscopy analyses revealed that in vitro HsCEP135-N interacts with tubulin, protofilaments, and microtubules and induces the formation of microtubule bundles |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
CEP135
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