| CENP-F-dependent DRP1 function regulates APC/C activity during oocyte meiosis I. | CENP-F-dependent DRP1 function regulates APC/C activity during oocyte meiosis I.
Zhou CJ, Wang XY, Dong YH, Wang DH, Han Z, Zhang XJ, Sun QY, Carroll J, Liang CG., Free PMC Article | 12/24/2022 |
| Apoptosis-induced translocation of centromere protein F in its corresponding autoantibody production in hepatocellular carcinoma. | Apoptosis-induced translocation of centromere protein F in its corresponding autoantibody production in hepatocellular carcinoma.
Li X, Li Y, Xu A, Zhou D, Zhang B, Qi S, Chen Z, Wang X, Ou X, Cao B, Qu C, Huang J., Free PMC Article | 11/6/2021 |
| Loss of CENPF leads to developmental failure in mouse embryos. | Loss of CENPF leads to developmental failure in mouse embryos.
Zhou CJ, Wang XY, Han Z, Wang DH, Ma YZ, Liang CG., Free PMC Article | 09/19/2020 |
| Loss of CENP-F Function Induces Kidney Enlargement. | Malformations in the Murine Kidney Caused by Loss of CENP-F Function.
Haley CO, Waters AM, Bader DM. | 04/4/2020 |
| Results found that loss of function mutation in CENPF results in dilated cardiomyopathy with significant disruption in the microtubule network of cardiac myocytes in mouse. | Loss of CENP-F Results in Dilated Cardiomyopathy with Severe Disruption of Cardiac Myocyte Architecture.
Manalo A, Schroer AK, Fenix AM, Shancer Z, Coogan J, Brolsma T, Burnette DT, Merryman WD, Bader DM., Free PMC Article | 10/12/2019 |
| Due to the multifunctionality of CENP-F, the cellular phenotypes observed upon its depletion are difficult to interpret and there is a need to genetically separate its different functions by preventing binding to selected partners. Here we engineer a CENP-F point-mutant that is deficient in Miro1/2 binding and thus is unable to localize to mitochondria, but retains other localizations. | Miro-dependent mitochondrial pool of CENP-F and its farnesylated C-terminal domain are dispensable for normal development in mice.
Peterka M, Kornmann B., Free PMC Article | 09/21/2019 |
| Our data show that mutation of the CENP-F gene leads to an unexpected hyperstabilization of the MT network, with a unique loss of dynamic instability. With disruption of MT dynamics, CENP-F-/- cells exhibit dramatic loss of directionally persistent migration, defects in focal adhesion disassembly and lamellipodial formation/retraction, change in cilia frequency, and loss of regulation of cell shape. | Loss of CENP-F results in distinct microtubule-related defects without chromosomal abnormalities.
Pfaltzgraff ER, Roth GM, Miller PM, Gintzig AG, Ohi R, Bader DM., Free PMC Article | 09/2/2017 |
| FOXM1 and CENPF are master regulators of prostate cancer malignancy, and can serve as drug response markers for antineoplastic drugs efficiency. | Predicting Drug Response in Human Prostate Cancer from Preclinical Analysis of In Vivo Mouse Models.
Mitrofanova A, Aytes A, Zou M, Shen MM, Abate-Shen C, Califano A., Free PMC Article | 07/16/2016 |
| Loss of CENP-F function in developing myocytes leads to decreased cell division, blunting of trabeculation and an initially smaller, thin-walled heart. | Cardiac-specific deletion of the microtubule-binding protein CENP-F causes dilated cardiomyopathy.
Dees E, Miller PM, Moynihan KL, Pooley RD, Hunt RP, Galindo CL, Rottman JN, Bader DM., Free PMC Article | 01/26/2013 |
| These data demonstrate that CMF1 regulates myocyte differentiation by interaction with Rb family members to induce expression of myogenic regulatory factors. | CMF1-Rb interaction promotes myogenesis in avian skeletal myoblasts.
Robertson JB, Zhu T, Nasreen S, Kilkenny D, Bader D, Dees E., Free PMC Article | 03/11/2011 |
| Data show that the post-anaphase, KEN-box-dependent degradation of Cenp-F requires it to be farnesylated, a post-translational modification usually linked to membrane association. | Cdc20 is required for the post-anaphase, KEN-dependent degradation of centromere protein F.
Gurden MD, Holland AJ, van Zon W, Tighe A, Vergnolle MA, Andres DA, Spielmann HP, Malumbres M, Wolthuis RM, Cleveland DW, Taylor SS., Free PMC Article | 05/3/2010 |
| Results identify Hook2, a linker protein that is essential for regulation of the microtubule network at the centrosome, as a binding partner of CENP-F. | Murine CENP-F regulates centrosomal microtubule nucleation and interacts with Hook2 at the centrosome.
Moynihan KL, Pooley R, Miller PM, Kaverina I, Bader DM., Free PMC Article | 02/15/2010 |
| CENPF and syntaxin 4 colocalize with components of plasma membrane recycling: SNAP-25 and VAMP2. Depletion of endogenous CENPF disrupts GLUT4 trafficking | Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport.
Pooley RD, Moynihan KL, Soukoulis V, Reddy S, Francis R, Lo C, Ma LJ, Bader DM., Free PMC Article | 01/21/2010 |
| LEK1 plays a prominent role in regulating dendritic cell (DC) function for T cell activation, since knockdown of LEK1 expression results in the rapid maturation of Chlamydia-exposed DCs as measured by analysis of key activation markers. | Involvement of LEK1 in dendritic cell regulation of T cell immunity against Chlamydia.
He Q, Eko FO, Lyn D, Ananaba GA, Bandea C, Martinez J, Joseph K, Kellar K, Black CM, Igietseme JU., Free PMC Article | 01/21/2010 |
| Results indicate that Raf-arrested myoblasts may serve as a model system for satellite cell cycle studies and that E2F5 and LEK1 translocation to the nucleus is an important first step during entry into quiescence. | E2F5 and LEK1 translocation to the nucleus is an early event demarcating myoblast quiescence.
Reed SA, Ouellette SE, Liu X, Allen RE, Johnson SE. | 01/21/2010 |
| The domains of the C-terminus of mCenp-F have a conserved function in control of mitotic progression through protein-protein interaction with pocket proteins. | Conserved C-terminal domains of mCenp-F (LEK1) regulate subcellular localization and mitotic checkpoint delay.
Evans HJ, Edwards L, Goodwin RL., Free PMC Article | 01/21/2010 |
| These data suggest a role for LEK1 in regulating the normal embryonic cardiomyocyte cell cycle and in promoting continued mitosis in transformed, abnormally dividing cardiomyocytes. | LEK1 protein expression in normal and dysregulated cardiomyocyte mitosis.
Dees E, Robertson JB, Ashe M, Pabón-Peña LM, Bader D, Goodwin RL. | 01/21/2010 |
| LEK1 specifically functions during murine development to regulate the activity of Rb proteins during cell division and proliferation. | LEK1 is a potential inhibitor of pocket protein-mediated cellular processes.
Ashe M, Pabon-Peña L, Dees E, Price KL, Bader D. | 01/21/2010 |