| Interacting proteins: P02545 and P01100 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02545 and P01100 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02545 and P01100 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02545 and P01100 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02545 and P01100 |
Pubmed |
SVM Score :0.0 |
| A mechanism of AP 1 suppression through interaction of c Fos with lamin A / C . ^^^ Here we show that the intermediate filament protein lamin A / C suppresses AP 1 function through direct interaction with c Fos , and that both proteins can interact and colocalize at the nuclear envelope ( NE ) in mammalian cells . ^^^ Notably , c Fos colocalizes with lamin A / C at the NE in starvation synchronized quiescent cells lacking detectable AP 1 DNA binding . ^^^ In contrast , serum induced AP 1 DNA binding activity coincides with abundant nucleoplasmic c Fos expression without changes in lamin A / C localization . ^^^ In contrast , lamin A overexpression causes growth arrest , and ectopic c Fos partially overcomes lamin A / C induced cell cycle alterations . ^^^ |
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| Interacting proteins: P02545 and P01100 |
Pubmed |
SVM Score :0.0 |
| This and preliminary observations on fos RNA accumulation suggests the possible existence of a genetic defect in HGPS fibroblasts . . ^^^ |
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