Specific interaction between Smad1 and CHIP: a surface plasmon resonance study.
The TGF-beta superfamily signaling pathway regulates many important biological processes, including cell growth, differentiation and embryonic pattern formation. Smad1, a member of this signaling pathway that functions downstream of serine/threonine kinase receptors, has ability to interact with carboxyl terminus of Hsc70-interacting protein (CHIP), which is an E3 ubiquitin ligase in other cases. It has been reported that Smurf1, a member of the Hect family E3 ubiquitin ligases, can target Smad1 to 26S proteasome for degradation. In this paper, we studied the interaction of Smad1 and CHIP by combination of surface plasmon resonance and supported monolayer approach. The specific binding of Smad1 to CHIP indicates that the degradation of Smad1 may also be mediated by CHIP, and CHIP may play an essential role in the TGF-beta signaling pathway.
Li
Ren-Feng
RF
Department of Biological Sciences and Biotechnology, State-Key Laboratory of Biomembrane, Tsinghua University, Beijing 100084, PR China.
Zhang
Fan
F
Lu
Ying-Jie
YJ
Sui
Sen-Fang
SF
D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D006639:Histidine; D006801:Humans; D007700:Kinetics; D008239:Lysine / Q000031:analogs & derivatives*; D009829:Oleic Acids; D051785:Smad Proteins; D051898:Smad1 Protein; D051901:Smad4 Protein; D013386:Succinates; D020349:Surface Plasmon Resonance; D015534:Trans-Activators / Q000737:chemistry / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry / Q000378:metabolism*
D004268:DNA-Binding Proteins; C476561:N(alpha),N(alpha)-bis(carboxymethyl)-N(epsilon)-(1,2-dioleyl-sn-glycero-3-succinyl)-L-lysine; D009829:Oleic Acids; C497399:SMAD1 protein, human; C497796:SMAD4 protein, human; D051785:Smad Proteins; D051898:Smad1 Protein; D051901:Smad4 Protein; D013386:Succinates; D015534:Trans-Activators; D006639:Histidine; C467728:STUB1 protein, human; D044767:Ubiquitin-Protein Ligases; D008239:Lysine