| functionally relevant miRNA/mRNA interactions were identified in skeletal muscles of myotonic dystrophy type 1 patients, highlighting the dysfunction of miR-29c and ASB2. | High-throughput analysis of the RNA-induced silencing complex in myotonic dystrophy type 1 patients identifies the dysregulation of miR-29c and its target ASB2.
Cappella M, Perfetti A, Cardinali B, Garcia-Manteiga JM, Carrara M, Provenzano C, Fuschi P, Cardani R, Renna LV, Meola G, Falcone G, Martelli F., Free PMC Article | 11/9/2019 |
| Notch signaling can initiate Asb2 transcription and NF-kappa B activation in T cell acute lymphoblastic leukemia cells. | The notch pathway promotes NF-κB activation through Asb2 in T cell acute lymphoblastic leukemia cells.
Wu W, Nie L, Zhang L, Li Y., Free PMC Article | 11/3/2018 |
| Using ASB2 conditional knockout mice. | Substrates of the ASB2α E3 ubiquitin ligase in dendritic cells.
Spinner CA, Uttenweiler-Joseph S, Metais A, Stella A, Burlet-Schiltz O, Moog-Lutz C, Lamsoul I, Lutz PG., Free PMC Article | 09/24/2016 |
| Phosphorylation of serine 323 of ASB2 alpha by Erk kinases is critical for ASB2alpha-mediated degradation of FLNA. | Phosphorylation of serine 323 of ASB2α is pivotal for the targeting of filamin A to degradation.
Zakaria R, Lamsoul I, Uttenweiler-Joseph S, Erard M, Monsarrat B, Burlet-Schiltz O, Moog-Lutz C, Lutz PG. | 12/6/2014 |
| data therefore reveal ubiquitin acceptor sites in FLNa and establish that ASB2alpha-mediated effects on cell spreading are due to loss of filamins. | ASB2α, an E3 ubiquitin ligase specificity subunit, regulates cell spreading and triggers proteasomal degradation of filamins by targeting the filamin calponin homology 1 domain.
Razinia Z, Baldassarre M, Cantelli G, Calderwood DA., Free PMC Article | 01/4/2014 |
| Data show that neither endogenous nor exogenously expressed ASB2alpha induces degradation of JAK proteins in hematopoietic cells | Filamins but not Janus kinases are substrates of the ASB2α cullin-ring E3 ubiquitin ligase in hematopoietic cells.
Lamsoul I, Erard M, van der Ven PF, Lutz PG., Free PMC Article | 01/26/2013 |
| These results suggest that ASB2beta but not ASB2alpha might be monoubiquitinated and that the ASB2beta UIM motif, but not its E3 Ub ligase activity, plays a pivotal role in this monoubiquitination. | The ASB2β Ubiquitin-interacting motif is involved in its monoubiquitination.
Nishiyama T, Kuroda S, Takiguchi E, Nakamura T, Hashimoto K, Tsuzuranuki K, Kawakami T, Masuho Y, Kohroki J. | 06/2/2012 |
| A model whereby ASB2 contributes to hematopoietic differentiation, in part, through MLL degradation and HOX gene down-regulation. | ECSASB2 mediates MLL degradation during hematopoietic differentiation.
Wang J, Muntean AG, Hess JL., Free PMC Article | 04/7/2012 |
| ASB2alpha is a novel regulator of integrin-dependent adhesion of hematopoietic cells | Functional and structural insights into ASB2alpha, a novel regulator of integrin-dependent adhesion of hematopoietic cells.
Lamsoul I, Burande CF, Razinia Z, Houles TC, Menoret D, Baldassarre M, Erard M, Moog-Lutz C, Calderwood DA, Lutz PG., Free PMC Article | 10/29/2011 |
| By shifting monomeric E3 ligase complexes to dimeric forms through activation of Asb2 transcription, Notch could effectively control the turnover of a variety of substrates and it exerts diverse effects on cell proliferation and differentiation. | Notch-induced Asb2 expression promotes protein ubiquitination by forming non-canonical E3 ligase complexes.
Nie L, Zhao Y, Wu W, Yang YZ, Wang HC, Sun XH., Free PMC Article | 09/3/2011 |
| ASB2 may regulate hematopoietic cell differentiation by modulating cell spreading and actin remodeling through targeting of filamins A and B for degradation. | ASB2 targets filamins A and B to proteasomal degradation.
Heuzé ML, Lamsoul I, Baldassarre M, Lad Y, Lévêque S, Razinia Z, Moog-Lutz C, Calderwood DA, Lutz PG., Free PMC Article | 01/21/2010 |