CIBICI 14215
CENTRO DE INVESTIGACION EN BIOQUIMICA CLINICA E INMUNOLOGIA
Unidad Ejecutora - UE
artículos
Título:
The E3 ubiquitin ligase mindbomb homolog 2 (Drosophila) (MIB2) protein controls B-cell CLL/Lymphoma 10 (BCL10)-dependent NF-êB activation
Autor/es:
STEMPIN, CC; CHI, L; HAECKER, H AND REDECKE V.
Revista:
JOURNAL OF BIOLOGICAL CHEMISTRY
Editorial:
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Referencias:
Año: 2011 vol. 286 p. 37147 - 37157
ISSN:
0021-9258
Resumen:
B-cell CLL/lymphoma 10 (BCL10) is crucial for the activation
of NF-B in numerous immune receptor signaling pathways,
including the T-cell receptor (TCR) and B-cell receptor signaling
pathways. However, the molecular mechanisms that lead to
signal transduction from BCL10 to downstream NF-B effector
kinases, such as TAK1 and components of the IKK complex, are
not entirely understood. Here we used a proteomic approach
and identified the E3 ligase MIB2 as a novel component of the
activated BCL10 complex. In vitro translation and pulldown assays
suggest direct interaction between BCL10 and MIB2. Overexpression
experiments show that MIB2 controls BCL10-mediated activation
of NF-B by promoting autoubiquitination and ubiquitination
of IKK/NEMO, as well as recruitment and activation of
TAK1. Knockdown of MIB2 inhibited BCL10-dependent NF-B
activation. Together, our results identify MIB2 as a novel componentoftheactivatedBCL10signalingcomplexandamissinglinkin
the BCL10-dependent NF-B signaling pathway.B in numerous immune receptor signaling pathways,
including the T-cell receptor (TCR) and B-cell receptor signaling
pathways. However, the molecular mechanisms that lead to
signal transduction from BCL10 to downstream NF-B effector
kinases, such as TAK1 and components of the IKK complex, are
not entirely understood. Here we used a proteomic approach
and identified the E3 ligase MIB2 as a novel component of the
activated BCL10 complex. In vitro translation and pulldown assays
suggest direct interaction between BCL10 and MIB2. Overexpression
experiments show that MIB2 controls BCL10-mediated activation
of NF-B by promoting autoubiquitination and ubiquitination
of IKK/NEMO, as well as recruitment and activation of
TAK1. Knockdown of MIB2 inhibited BCL10-dependent NF-B
activation. Together, our results identify MIB2 as a novel componentoftheactivatedBCL10signalingcomplexandamissinglinkin
the BCL10-dependent NF-B signaling pathway.B effector
kinases, such as TAK1 and components of the IKK complex, are
not entirely understood. Here we used a proteomic approach
and identified the E3 ligase MIB2 as a novel component of the
activated BCL10 complex. In vitro translation and pulldown assays
suggest direct interaction between BCL10 and MIB2. Overexpression
experiments show that MIB2 controls BCL10-mediated activation
of NF-B by promoting autoubiquitination and ubiquitination
of IKK/NEMO, as well as recruitment and activation of
TAK1. Knockdown of MIB2 inhibited BCL10-dependent NF-B
activation. Together, our results identify MIB2 as a novel componentoftheactivatedBCL10signalingcomplexandamissinglinkin
the BCL10-dependent NF-B signaling pathway.In vitro translation and pulldown assays
suggest direct interaction between BCL10 and MIB2. Overexpression
experiments show that MIB2 controls BCL10-mediated activation
of NF-B by promoting autoubiquitination and ubiquitination
of IKK/NEMO, as well as recruitment and activation of
TAK1. Knockdown of MIB2 inhibited BCL10-dependent NF-B
activation. Together, our results identify MIB2 as a novel componentoftheactivatedBCL10signalingcomplexandamissinglinkin
the BCL10-dependent NF-B signaling pathway.B by promoting autoubiquitination and ubiquitination
of IKK/NEMO, as well as recruitment and activation of
TAK1. Knockdown of MIB2 inhibited BCL10-dependent NF-B
activation. Together, our results identify MIB2 as a novel componentoftheactivatedBCL10signalingcomplexandamissinglinkin
the BCL10-dependent NF-B signaling pathway.B
activation. Together, our results identify MIB2 as a novel componentoftheactivatedBCL10signalingcomplexandamissinglinkin
the BCL10-dependent NF-B signaling pathway.B signaling pathway.
