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Details on Person The phosphorylated C-terminal tail of R-SMAD induces a confo...

Class:IdSummation:176014
_displayNameThe phosphorylated C-terminal tail of R-SMAD induces a confo...
_timestamp2021-07-07 12:27:45
created[InstanceEdit:176006] Jassal, B, 2006-02-28 10:02:50
literatureReference[LiteratureReference:175954] TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4
[LiteratureReference:1225903] Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors
[LiteratureReference:202606] Structural basis of Smad1 activation by receptor kinase phosphorylation
[LiteratureReference:208376] Structural basis of heteromeric smad protein assembly in TGF-beta signaling
[LiteratureReference:3009206] Endofin, a FYVE domain protein, interacts with Smad4 and facilitates transforming growth factor-beta signaling
modified[InstanceEdit:176037] Jassal, B, 2006-03-01 09:45:45
[InstanceEdit:203064] Jassal, B, 2007-11-12 14:34:26
[InstanceEdit:1433619] May, B, 2011-07-12
[InstanceEdit:1529117] May, B, 2011-08-24
[InstanceEdit:1530039] Orlic-Milacic, Marija, 2011-08-25
[InstanceEdit:2197661] Orlic-Milacic, M, 2012-04-13
[InstanceEdit:2197665] Orlic-Milacic, M, 2012-04-13
[InstanceEdit:2197822] Orlic-Milacic, M, 2012-04-16
[InstanceEdit:3009209] Orlic-Milacic, M, 2013-02-04
[InstanceEdit:9736370] Shamovsky, Veronica, 2021-07-07
textThe phosphorylated C-terminal tail of R-SMAD induces a conformational change in the MH2 domain (Qin et al. 2001, Chacko et al. 2004), which now acquires high affinity towards Co-SMAD i.e. SMAD4 (common mediator of signal transduction in TGF-beta/BMP signaling). The R-SMAD:Co-SMAD complex (Nakao et al. 1997) most likely is a trimer of two R-SMADs with one Co-SMAD (Kawabata et al. 1998). It is important to note that the Co-SMAD itself cannot be phosphorylated as it lacks the C-terminal serine motif.

ZFYVE16 (endofin) promotes SMAD heterotrimer formation. ZFYVE16 can bind TGFBR1 and facilitate SMAD2 phosphorylation, and it can also bind SMAD4, but the exact mechanism of ZFYVE16 (endofin) action in the context of TGF-beta receptor signaling is not known (Chen et al. 2007).

SARS-CoV-1 nucleocapsid protein (N) associates with SMAD3 and this binding interferes with the complex formation between SMAD3 and SMAD4. By this mechanism N modulates TGF-beta signaling to block apoptosis of SARS-CoV-infected host cells (Zhao et al. 2008).

(summation)[Reaction:170847] Phosphorylated SMAD2 and SMAD3 form a complex with SMAD4 [Homo sapiens]
[Reaction:201422] Phospho-R-Smad1/5/8 forms a complex with Co-Smad [Homo sapiens]
[Reaction:9846183] GOCAM Phosphorylated SMAD2 and SMAD3 form a complex with SMAD4 [Homo sapiens]
[Reaction:9846552] GOCAM Phosphorylated SMAD2 and SMAD3 form a complex with SMAD4 [Homo sapiens]
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