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Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decay.
The SMG-1-mediated phosphorylation of Upf1 occurs on the association of SURF with EJC, which provides the link between the EJC and recognition of PTCs and triggers NMD.
Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes containing hSMG-5 and hSMG-7.
PAR-6–PAR-3 mediates Cdc42-induced Rac activation through the Rac GEFs STEF/Tiam1
It is proposed that the PAR-6–PAR-3 complex mediates Cdc42-induced Rac activation by means of STEF/Tiam1, and that this process seems to be required for the establishment of neuronal polarity.
The PAR-aPKC system: lessons in polarity
Accumulating evidence has revealed that mechanisms by which the asymmetrically localized components of the PAR-aPKC system are linked with other cellular machinery for developing polarity are divergent depending on the cell type.
Protein Kinase C δ Activates the MEK-ERK Pathway in a Manner Independent of Ras and Dependent on Raf*
- Y. Ueda, S. Hirai, S. Osada, A. Suzuki, K. Mizuno, S. Ohno
- Biology, Computer ScienceThe Journal of Biological Chemistry
- 20 September 1996
Results demonstrate that activation of PKCδ is sufficient for the activation of MEK and ERK and that the pathway operates in a manner dependent on c-Raf and independent of Ras.
An Atypical PKC Directly Associates and Colocalizes at the Epithelial Tight Junction with ASIP, a Mammalian Homologue of Caenorhabditis elegans Polarity Protein PAR-3
A role for a protein complex containing ASIP and aPKC in the establishment and/or maintenance of epithelial cell polarity is suggested and its asymmetric distribution in polarized cells from worm embryo to mammalian-differentiated cells may mean that the complex functions generally in the organization of cellular asymmetry.
Mammalian Lgl Forms a Protein Complex with PAR-6 and aPKC Independently of PAR-3 to Regulate Epithelial Cell Polarity
Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans.
It is reported that an atypical protein kinase C (PKC-3) is essential for proper asymmetric cell divisions and co-localizes with PAR-3 and concludes that PKC-3 plays an indispensable role in establishing embryonic polarity through interaction withPAR-3.
Polarity-Dependent Distribution of Angiomotin Localizes Hippo Signaling in Preimplantation Embryos
Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA…
It is concluded that h SMG-1 plays a critical role in NMD through the direct phosphorylation of hUPF1/SMG-2 in the evolutionally conserved mRNA surveillance complex.