S
Shirin Abdollah
Researcher at University of Toronto
Publications - 6
Citations - 4305
Shirin Abdollah is an academic researcher from University of Toronto. The author has contributed to research in topics: TGF beta signaling pathway & Smad2 Protein. The author has an hindex of 6, co-authored 6 publications receiving 4206 citations. Previous affiliations of Shirin Abdollah include Mount Sinai Hospital.
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Journal ArticleDOI
The MAD-Related Protein Smad7 Associates with the TGFβ Receptor and Functions as an Antagonist of TGFβ Signaling
Hidetoshi Hayashi,Shirin Abdollah,Yubin Qiu,Jiexing Cai,Yong-Yao Xu,Brian W. Grinnell,Mark A. Richardson,James N. Topper,Michael A. Gimbrone,Jeffrey L. Wrana,Dean A. Falb +10 more
TL;DR: A novel function for MAD-related proteins as intracellular antagonists of the type I kinase domain of TGFβ family receptors is defined as blocking the association, phosphorylation, and activation of Smad2.
Journal ArticleDOI
A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation.
Haitao Zhu,Peter A. Kavsak,Peter A. Kavsak,Shirin Abdollah,Shirin Abdollah,Jeffrey L. Wrana,Jeffrey L. Wrana,Gerald H. Thomsen +7 more
TL;DR: Smurf1, a new member of the Hect family of E3 ubiquitin ligases, selectively interacts with receptor-regulated SMADs specific for the BMP pathway in order to trigger their ubiquitination and degradation, and hence their inactivation.
Journal ArticleDOI
MADR2 Is a Substrate of the TGFβ Receptor and Its Phosphorylation Is Required for Nuclear Accumulation and Signaling
Marina Macías-Silva,Shirin Abdollah,Pamela A. Hoodless,Rosa Pirone,Liliana Attisano,Jeffrey L. Wrana +5 more
TL;DR: It is demonstrated that MADR2 and not the related protein DPC4 transiently interacts with the TGFbeta receptor and is directly phosphorylated by the complex on C-terminal serines.
Journal ArticleDOI
MADR1, a MAD-Related Protein That Functions in BMP2 Signaling Pathways
Pamela A. Hoodless,Theo Haerry,Shirin Abdollah,Mark Stapleton,Michael B. O'Connor,Liliana Attisano,Jeffrey L. Wrana +6 more
TL;DR: It is shown that MAD functions downstream of DPP receptors and is required for receptor signaling, and may define a novel class of signaling molecules with nuclear function in Ser/Thr kinase receptor signaling pathways.
Journal ArticleDOI
TβRI Phosphorylation of Smad2 on Ser465 and Ser467 Is Required for Smad2-Smad4 Complex Formation and Signaling
Shirin Abdollah,Marina Macías-Silva,Tomoo Tsukazaki,Hidetoshi Hayashi,Liliana Attisano,Jeffrey L. Wrana +5 more
TL;DR: Results indicate that receptor-dependent phosphorylation of Smad2 on serines 465 and 467 is required in mammalian cells to permit association with Smad4 and to propagate TGF-β signals.