Abstract：
:SARA, an early endosomal protein, plays a key role in TGFβ signalling, as it presents SMAD2 and SMAD3 for phosphorylation by the activated TGFβ receptors. Here, we show that ERBIN is a new SARA-interacting protein that can be recruited by SARA to early endosomes. ERBIN was recently shown to bind and segregate phosphorylated SMAD2 and SMAD3 (SMAD2/3) in the cytoplasm, thereby inhibiting SMAD2/3-dependent transcription. SARA binds to ERBIN using a new domain, which we have called the ERBID (ERBIN-binding domain), whereas ERBIN binds to SARA using a domain (amino acids 1208-1265) that also interacts with SMAD2 and SMAD3, which we have called the SSID (SARA- and SMAD-interacting domain). We additionally show that SARA competes with SMAD2/3 for binding to ERBIN. In agreement, overexpression of SARA or the ERBID peptide reverses the inhibitory effect of ERBIN on SMAD2/3-dependent transcription. Taken together, these data suggest that the response of cells to TGFβ and activin A can be influenced by the relative concentrations of SARA, ERBIN and SMAD2/3.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Sflomos G,Kostaras E,Panopoulou E,Pappas N,Kyrkou A,Politou AS,Fotsis T,Murphy Cdoi
10.1242/jcs.062307subject
Has Abstractpub_date
2011-10-01 00:00:00pages
3209-22issue
Pt 19eissn
0021-9533issn
1477-9137pii
jcs.062307journal_volume
124pub_type
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