Sclerostin–erbB-3 interactions: Modulation of erbB-3 activity by sclerostin
نویسندگان
چکیده
منابع مشابه
c-erbB-3
c-erbB receptors are usually located in cell membranes and are activated by extracellular binding of EGF-like growth factors. Unexpectedly, using immunofluorescence we found high levels of c-erbB-3 within the nuclei of MTSV1-7 immortalized nonmalignant human mammary epithelial cells. Nuclear localization was mediated by the COOH terminus of c-erbB-3, and a nuclear localization signal was identi...
متن کاملErbB 3 is an active tyrosine kinase capable of homo - and hetero - interactions 2 3
1 ErbB3 is an active tyrosine kinase capable of homoand hetero-interactions 2 3 Mara P. Steinkamp a,c , Shalini T. Low-Nam a *, Shujie Yang a▲ , 4 Keith A. Lidke b,c , Diane S. Lidke a,c and Bridget S. Wilson a,c# 5 6 Department of Pathology a , Department of Physics b and Cancer Center c 7 University of New Mexico, Albuquerque, New Mexico 87131 8 9 10 11 12 13 Running Head: erbB3 participates ...
متن کاملSelective formation of ErbB-2/ErbB-3 heterodimers depends on the ErbB-3 affinity of epidermal growth factor-like ligands.
EGF-like growth factors activate their ErbB receptors by promoting receptor-mediated homodimerization or, alternatively, by the formation of heterodimers with the orphan ErbB-2 through an as yet unknown mechanism. To investigate the selectivity in dimer formation by ligands, we have applied the phage display approach to obtain ligands with modified C-terminal residues that discriminate between ...
متن کاملTLR 3 modulation of hippocampal synaptic activity
9.40 am Motion integration times in sensory cortex are dynamically modified in response to changes in stimulus reliability 10.20 am Mapping molecular diversity of excitatory synapses in the mammalian brain 11.15 am Antidepressant effects on neuronal population dynamics : insights into the role of hippocampus in stress response and adaptive behaviours 11.35 am Preclinical modeling of chronic cen...
متن کاملModulation, via protein-protein interactions, of glyceraldehyde-3-phosphate dehydrogenase activity through redox phosphoribulokinase regulation.
The activity of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) embedded in the phosphoribulokinase (PRK).GAPDH.CP12 complex was increased 2-3-fold by reducing agents. This occurred by interaction with PRK as the cysteinyl sulfhydryls (4 SH/subunit) of GAPDH within the complex were unchanged whatever the redox state of the complex. But isolated GAPDH was not activated. Alkylation plus mass spe...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 2010
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2010.10.048