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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization.

Smad proteins mediate the transforming growth factor beta responses. C-terminal phosphorylation of R-Smads leads to the recruitment of Smad4 and the formation of active signaling complexes. We investigated the mechanism of phosphorylation-induced Smad complex formation with an activating pseudo- phosphorylated Smad3. Pseudo-phosphorylated Smad3 has a greater propensity to homotrimerize, and recruits Smad4 to form a heterotrimer containing two Smad3 and one Smad4. The trimeric interaction is mediated through conserved interfaces to which tumorigenic mutations map. Furthermore, a conserved Arg residue within the L3 loop, located near the C-terminal phosphorylation sites of the neighboring subunit, is essential for trimerization. We propose that the phosphorylated C-terminal residues interact with the L3 loop of the neighboring subunit to stabilize the trimer interaction.[1]

References

  1. The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization. Chacko, B.M., Qin, B., Correia, J.J., Lam, S.S., de Caestecker, M.P., Lin, K. Nat. Struct. Biol. (2001) [Pubmed]
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